| Year |
Citation |
Score |
| 2002 |
Butler C, Forte E, Maria Scandurra F, Arese M, Giuffré A, Greenwood C, Sarti P. Cytochrome bo(3) from Escherichia coli: the binding and turnover of nitric oxide. Biochemical and Biophysical Research Communications. 296: 1272-8. PMID 12207912 DOI: 10.1016/S0006-291X(02)02074-0 |
0.345 |
|
| 1999 |
Giuffrè A, Watmough NJ, Giannini S, Brunori M, Konings WN, Greenwood C. Electron transfer kinetics of caa3 oxidase from Bacillus stearothermophilus: a hypothesis for thermophilicity. Biophysical Journal. 76: 438-42. PMID 9876155 DOI: 10.1016/S0006-3495(99)77210-3 |
0.41 |
|
| 1998 |
ATHERTON NM, GIBSON QH, GREENWOOD C. Electronspin-resonance changes on oxidation of cytochrome oxidase. The Biochemical Journal. 86: 554-5. PMID 13965340 DOI: 10.1042/bj0860554 |
0.47 |
|
| 1998 |
GIBSON QH, GREENWOOD C. Reactions of cytochrome oxidase with oxygen and carbon monoxide. The Biochemical Journal. 86: 541-54. PMID 13947736 DOI: 10.1042/bj0860541 |
0.452 |
|
| 1998 |
Watmough NJ, Cheesman MR, Butler CS, Little RH, Greenwood C, Thomson AJ. The dinuclear center of cytochrome bo3 from Escherichia coli. Journal of Bioenergetics and Biomembranes. 30: 55-62. PMID 9623806 DOI: 10.1023/A:1020507511285 |
0.401 |
|
| 1997 |
Butler CS, Seward HE, Greenwood C, Thomson AJ. Fast cytochrome bo from Escherichia coli binds two molecules of nitric oxide at CuB. Biochemistry. 36: 16259-66. PMID 9405060 DOI: 10.1021/Bi971481A |
0.426 |
|
| 1997 |
Butler CS, Cheesman MR, Greenwood C, Thomson AJ, Watmough NJ. Fast cytochrome bo from Escherichia coli reacts with azide and nitric oxide to form a complex analogous to that formed by cytochrome c oxidase. Biochemical Society Transactions. 25: 392S. PMID 9388622 DOI: 10.1042/Bst025392S |
0.4 |
|
| 1997 |
Watmough NJ, Katsonouri A, Little RH, Osborne JP, Furlong-Nickels E, Gennis RB, Brittain T, Greenwood C. A conserved glutamic acid in helix VI of cytochrome bo3 influences a key step in oxygen reduction. Biochemistry. 36: 13736-42. PMID 9354645 DOI: 10.1021/Bi971434I |
0.365 |
|
| 1997 |
Brittain T, Hofmann OM, Watmough NJ, Greenwood C, Weber RE. A two-state analysis of co-operative oxygen binding in the three human embryonic haemoglobins. The Biochemical Journal. 326: 299-303. PMID 9291096 DOI: 10.1042/Bj3260299 |
0.326 |
|
| 1996 |
Brittain T, Little RH, Greenwood C, Watmough NJ. The reaction of Escherichia coli cytochrome bo with H2O2: evidence for the formation of an oxyferryl species by two distinct routes. Febs Letters. 399: 21-5. PMID 8980111 DOI: 10.1016/S0014-5793(96)01253-7 |
0.368 |
|
| 1996 |
Little RH, Cheesman MR, Thomson AJ, Greenwood C, Watmough NJ. Cytochrome bo from Escherichia coli: binding of azide to CuB. Biochemistry. 35: 13780-7. PMID 8901520 DOI: 10.1021/Bi961221D |
0.378 |
|
| 1995 |
Fülöp V, Ridout CJ, Greenwood C, Hajdu J. Crystal structure of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Structure (London, England : 1993). 3: 1225-33. PMID 8591033 DOI: 10.1016/S0969-2126(01)00258-1 |
0.402 |
|
| 1995 |
Lappalainen P, Watmough NJ, Greenwood C, Saraste M. Electron transfer between cytochrome c and the isolated CuA domain: identification of substrate-binding residues in cytochrome c oxidase. Biochemistry. 34: 5824-30. PMID 7727443 DOI: 10.1021/Bi00017A014 |
0.425 |
|
| 1994 |
Cheesman MR, Watmough NJ, Gennis RB, Greenwood C, Thomson AJ. Magnetic-circular-dichroism studies of Escherichia coli cytochrome bo. Identification of high-spin ferric, low-spin ferric and ferryl [Fe(IV)] forms of heme o. European Journal of Biochemistry / Febs. 219: 595-602. PMID 8307024 DOI: 10.1111/J.1432-1033.1994.Tb19975.X |
0.351 |
|
| 1994 |
Watmough NJ, Cheesman MR, Greenwood C, Thomson AJ. Cytochrome bo from Escherichia coli: reaction of the oxidized enzyme with hydrogen peroxide. The Biochemical Journal. 300: 469-75. PMID 8002953 DOI: 10.1042/Bj3000469 |
0.435 |
|
| 1993 |
Fülöp V, Little R, Thompson A, Greenwood C, Hajdu J. Crystallization and preliminary X-ray analysis of the di-haem cytochrome c peroxidase from Pseudomonas aeruginosa. Journal of Molecular Biology. 232: 1208-10. PMID 8396649 DOI: 10.1006/Jmbi.1993.1472 |
0.335 |
|
| 1993 |
Davies AM, Guillemette JG, Smith M, Greenwood C, Thurgood AG, Mauk AG, Moore GR. Redesign of the interior hydrophilic region of mitochondrial cytochrome c by site-directed mutagenesis. Biochemistry. 32: 5431-5. PMID 8388720 DOI: 10.1021/Bi00071A019 |
0.374 |
|
| 1993 |
Watmough NJ, Cheesman MR, Gennis RB, Greenwood C, Thomson AJ. Distinct forms of the haem o-Cu binuclear site of oxidised cytochrome bo from Escherichia coli. Evidence from optical and EPR spectroscopy. Febs Letters. 319: 151-4. PMID 8384121 DOI: 10.1016/0014-5793(93)80056-Z |
0.349 |
|
| 1993 |
Cheesman MR, Watmough NJ, Pires CA, Turner R, Brittain T, Gennis RB, Greenwood C, Thomson AJ. Cytochrome bo from Escherichia coli: identification of haem ligands and reaction of the reduced enzyme with carbon monoxide. The Biochemical Journal. 289: 709-18. PMID 8382047 DOI: 10.1042/Bj2890709 |
0.436 |
|
| 1993 |
Greenwood C, Brittain T, James R, Jaffar I, Little R, Thompson A, Fulop V. Structure function studies on pseudomonas cytochrome c peroxidase (PsCCP) Journal of Inorganic Biochemistry. 51: 181. DOI: 10.1016/0162-0134(93)85217-V |
0.343 |
|
| 1992 |
Brittain T, Blackmore R, Greenwood C, Thomson AJ. Bacterial nitrite-reducing enzymes. European Journal of Biochemistry / Febs. 209: 793-802. PMID 1425687 DOI: 10.1111/J.1432-1033.1992.Tb17350.X |
0.311 |
|
| 1992 |
Cheesman MR, Kadir FH, al-Basseet J, al-Massad F, Farrar J, Greenwood C, Thomson AJ, Moore GR. E.p.r. and magnetic circular dichroism spectroscopic characterization of bacterioferritin from Pseudomonas aeruginosa and Azotobacter vinelandii. The Biochemical Journal. 286: 361-7. PMID 1326939 DOI: 10.1042/Bj2860361 |
0.367 |
|
| 1992 |
Brittain T, Greenwood C. Complex formation between the copper protein, azurin and the cytochrome c peroxidase of Pseudomonas aeruginosa. Journal of Inorganic Biochemistry. 48: 71-7. PMID 1326600 DOI: 10.1016/0162-0134(92)80055-Z |
0.407 |
|
| 1992 |
Foote N, Turner R, Brittain T, Greenwood C. A quantitative model for the mechanism of action of the cytochrome c peroxidase of Pseudomonas aeruginosa. The Biochemical Journal. 283: 839-43. PMID 1317165 DOI: 10.1042/Bj2830839 |
0.372 |
|
| 1991 |
Thurgood AG, Davies AM, Greenwood C, Mauk AG, Smith M, Guillemette JG, Moore GR. NMR study of the structural characteristics of variants of yeast iso-1-cytochrome c in which unvaried aromatic residues have been substituted. European Journal of Biochemistry / Febs. 202: 339-47. PMID 1662130 DOI: 10.1111/J.1432-1033.1991.Tb16381.X |
0.356 |
|
| 1991 |
Thurgood AG, Pielak GJ, Cutler RL, Davies AM, Greenwood C, Mauk AG, Smith M, Williamson DJ, Moore GR. Change in charge of an unvaried heme contact residue does not cause a major change of conformation in cytochrome c. Febs Letters. 284: 173-7. PMID 1647980 DOI: 10.1016/0014-5793(91)80678-V |
0.327 |
|
| 1990 |
Blackmore RS, Brittain T, Greenwood C. An analysis of the reaction kinetics of the hexahaem nitrite reductase of the anaerobic rumen bacterium Wolinella succinogenes. The Biochemical Journal. 271: 457-61. PMID 2241924 DOI: 10.1042/Bj2710457 |
0.399 |
|
| 1990 |
Blackmore RS, Brittain T, Gadsby PM, Greenwood C, Thomson AJ. Two structurally and kinetically distinct forms of Wolinella succinogenes nitrite reductase. The Biochemical Journal. 271: 259-64. PMID 2171501 DOI: 10.1042/Bj2710259 |
0.332 |
|
| 1990 |
Blackmore RS, Gadsby PM, Greenwood C, Thomson AJ. The effect of haem ligands on the redox states of the hexa-haem nitrite reductase from Wolinella succinogenes. The Biochemical Journal. 271: 253-7. PMID 2171500 DOI: 10.1042/Bj2710253 |
0.356 |
|
| 1990 |
Cheesman MR, Thomson AJ, Greenwood C, Moore GR, Kadir F. Bis-methionine axial ligation of haem in bacterioferritin from Pseudomonas aeruginosa. Nature. 346: 771-3. PMID 2167456 DOI: 10.1038/346771A0 |
0.391 |
|
| 1990 |
Blackmore RS, Gadsby PM, Greenwood C, Thomson AJ. Spectroscopic studies of partially reduced forms of Wolinella succinogenes nitrite reductase. Febs Letters. 264: 257-62. PMID 2162787 DOI: 10.1016/0014-5793(90)80262-H |
0.373 |
|
| 1989 |
Foote N, Gadsby PM, Greenwood C, Thomson AJ. pH-dependent forms of the ferryl haem in myoglobin peroxide analysed by variable-temperature magnetic circular dichroism. The Biochemical Journal. 261: 515-22. PMID 2775230 DOI: 10.1042/Bj2610515 |
0.417 |
|
| 1988 |
Greenwood C, Thomson AJ, Barrett CP, Peterson J, George GN, Fee JA, Reichardt J. Some spectroscopic views of the CuA site in cytochrome c oxidase preparations. Annals of the New York Academy of Sciences. 550: 47-52. PMID 2854410 DOI: 10.1111/J.1749-6632.1988.Tb35321.X |
0.371 |
|
| 1987 |
Foote N, Gadsby PM, Field RA, Greenwood C, Thomson AJ. A comparison by magnetic circular dichroism of compound X and compound II of horseradish peroxidase. Febs Letters. 214: 347-50. PMID 3569529 DOI: 10.1016/0014-5793(87)80085-6 |
0.31 |
|
| 1987 |
Godfrey C, Gadsby PM, Thomson AJ, Greenwood C, Coddington A. Electron-paramagnetic-resonance and magnetic-circular-dichroism studies on the formate dehydrogenase-nitrate reductase particle from Pseudomonas aeruginosa. The Biochemical Journal. 243: 241-8. PMID 3038083 DOI: 10.1042/Bj2430241 |
0.371 |
|
| 1987 |
Gadsby PM, Greenwood C, Coddington A, Thomson AJ, Godfrey C. Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Electron-paramagnetic-resonance studies on the molybdenum centre. The Biochemical Journal. 243: 235-9. PMID 3038082 DOI: 10.1042/Bj2430235 |
0.337 |
|
| 1987 |
Godfrey C, Coddington A, Greenwood C, Thomson AJ, Gadsby PM. Purification and properties of formate dehydrogenase from Pseudomonas aeruginosa. Characterization of haem and iron-sulphur centres by magnetic-circular-dichroism and electron-paramagnetic-resonance spectroscopy. The Biochemical Journal. 243: 225-33. PMID 3038081 DOI: 10.1042/Bj2430225 |
0.44 |
|
| 1987 |
Blackmore RS, Brittain T, Gadsby PM, Greenwood C, Thomson AJ. Electron paramagnetic resonance and magnetic circular dichroism studies of a hexa-heme nitrite reductase from Wolinella succinogenes. Febs Letters. 219: 244-8. PMID 3036599 DOI: 10.1016/0014-5793(87)81225-5 |
0.357 |
|
| 1987 |
Thomson AJ, Greenwood C, Peterson J, Barrett CP. Determination of the optical properties of CuA(II) in bovine cytochrome c oxidase using magnetic circular dichroism as an optical detector of paramagnetic resonance. Journal of Inorganic Biochemistry. 28: 195-205. PMID 3027254 DOI: 10.1016/0162-0134(86)80083-6 |
0.331 |
|
| 1987 |
Foote N, Gadsby PM, Berry MJ, Greenwood C, Thomson AJ. The formation of ferric haem during low-temperature photolysis of horseradish peroxidase Compound I. The Biochemical Journal. 246: 659-68. PMID 2825645 DOI: 10.1042/Bj2460659 |
0.4 |
|
| 1987 |
Gadsby PM, Peterson J, Foote N, Greenwood C, Thomson AJ. Identification of the ligand-exchange process in the alkaline transition of horse heart cytochrome c. The Biochemical Journal. 246: 43-54. PMID 2823795 DOI: 10.1042/Bj2460043 |
0.417 |
|
| 1986 |
Hill BC, Greenwood C, Nicholls P. Intermediate steps in the reaction of cytochrome oxidase with molecular oxygen Biochimica Et Biophysica Acta. 853: 91-113. PMID 3030416 DOI: 10.1016/0304-4173(86)90006-6 |
0.32 |
|
| 1986 |
Sutherland J, Greenwood C, Peterson J, Thomson AJ. An investigation of the ligand-binding properties of Pseudomonas aeruginosa nitrite reductase. The Biochemical Journal. 233: 893-8. PMID 3010946 DOI: 10.1042/Bj2330893 |
0.432 |
|
| 1985 |
Hill BC, Woon TC, Nicholls P, Peterson J, Greenwood C, Thomson AJ. Interactions of sulphide and other ligands with cytochrome c oxidase. An electron-paramagnetic-resonance study. The Biochemical Journal. 224: 591-600. PMID 6097224 DOI: 10.1042/Bj2240591 |
0.404 |
|
| 1985 |
Foote N, Peterson J, Gadsby PM, Greenwood C, Thomson AJ. Redox-linked spin-state changes in the di-haem cytochrome c-551 peroxidase from Pseudomonas aeruginosa. The Biochemical Journal. 230: 227-37. PMID 2996492 DOI: 10.1042/Bj2300227 |
0.398 |
|
| 1985 |
Thomson AJ, Greenwood C, Gadsby PM, Peterson J, Eglinton DG, Hill BC, Nicholls P. The structure of the cytochrome a3-CuB site of mammalian cytochrome c oxidase as probed by MCD and EPR spectroscopy. Journal of Inorganic Biochemistry. 23: 187-97. PMID 2991457 DOI: 10.1016/0162-0134(85)85025-X |
0.363 |
|
| 1985 |
GREENWOOD C, FOOTE N, PETERSON J, THOMSON A. Photolytic studies on cytochrome c peroxidase from Pseudomonas aeruginosa Biochemical Society Transactions. 13: 625-626. DOI: 10.1042/Bst0130625 |
0.391 |
|
| 1984 |
Eglinton DG, Hill BC, Greenwood C, Thomson AJ. Low temperature magnetic circular dichroism spectra and magnetization properties of extracted heme a3+ bis-imidazole. A model of cytochrome a in bovine cytochrome c oxidase. Journal of Inorganic Biochemistry. 21: 1-8. PMID 6327904 DOI: 10.1016/0162-0134(84)85034-5 |
0.361 |
|
| 1984 |
Hill BC, Greenwood C. Kinetic evidence for the re-definition of electron transfer pathways from cytochrome c to O2 within cytochrome oxidase Febs Letters. 166: 362-366. PMID 6319198 DOI: 10.1016/0014-5793(84)80113-1 |
0.448 |
|
| 1984 |
Greenwood C, Hill BC, Barber D, Eglinton DG, Thomson AJ. The optical properties of CuA in bovine cytochrome c oxidase determined by low-temperature magnetic-circular-dichroism spectroscopy. The Biochemical Journal. 215: 303-16. PMID 6316924 DOI: 10.1042/Bj2150303 |
0.404 |
|
| 1984 |
Godfrey C, Greenwood C, Thomson AJ, Bray RC, George GN. Electron-paramagnetic-resonance spectroscopy studies on the dissimilatory nitrate reductase from Pseudomonas aeruginosa. The Biochemical Journal. 224: 601-8. PMID 6097225 DOI: 10.1042/Bj2240601 |
0.305 |
|
| 1984 |
Greenwood C, Foote N, Peterson J, Thomson AJ. The nature of species prepared by photolysis of half-reduced, fully reduced and fully reduced carbonmonoxy-cytochrome c-551 peroxidase from Pseudomonas aeruginosa. The Biochemical Journal. 223: 379-91. PMID 6093774 DOI: 10.1042/Bj2230379 |
0.371 |
|
| 1984 |
Foote N, Peterson J, Gadsby PM, Greenwood C, Thomson AJ. A study of the oxidized form of Pseudomonas aeruginosa cytochrome c-551 peroxidase with the use of magnetic circular dichroism. The Biochemical Journal. 223: 369-78. PMID 6093773 DOI: 10.1042/Bj2230369 |
0.38 |
|
| 1983 |
Hill BC, Brittain T, Eglinton DG, Gadsby PM, Greenwood C, Nicholls P, Peterson J, Thomson AJ, Woon TC. Low-spin ferric forms of cytochrome a3 in mixed-ligand and partially reduced cyanide-bound derivatives of cytochrome c oxidase. The Biochemical Journal. 215: 57-66. PMID 6312973 DOI: 10.1042/Bj2150057 |
0.45 |
|
| 1983 |
Foote N, Thompson AC, Barber D, Greenwood C. Pseudomonas cytochrome C-551 peroxidase. A purification procedure and study of CO-binding kinetics. The Biochemical Journal. 209: 701-7. PMID 6307263 DOI: 10.1042/Bj2090701 |
0.402 |
|
| 1983 |
Thomson AJ, Englinton DG, Hill BC, Greenwood C. The nature of haem a3 in the oxidized state of cytochrome c oxidase. Evidence from low-temperature magnetic-circular-dichroism spectroscopy in the near infrared region. The Biochemical Journal. 207: 167-70. PMID 6295364 DOI: 10.1042/Bj2070167 |
0.44 |
|
| 1982 |
Brittain T, Barber D, Greenwood C, Wells RM. An investigation of the co-operative binding of carbon monoxide to the haemoglobin of the carpet shark Cephaloscyllium. Comparative Biochemistry and Physiology B. 72: 689-693. PMID 7128118 DOI: 10.1016/0305-0491(82)90528-4 |
0.33 |
|
| 1982 |
Brittain T, Barber D, Greenwood C, Wells RM. An investigation of the allosteric functioning of the haemoglobin of the cane toad, Bufo marinus. Comparative Biochemistry and Physiology B. 73: 991-995. PMID 6817967 DOI: 10.1016/0305-0491(82)90348-0 |
0.319 |
|
| 1982 |
Johnson MK, Eglinton DG, Gooding PE, Greenwood C, Thomson AJ. Characterization of the partially reduced cyanide-inhibited derivative of cytochrome c oxidase by optical, electron-paramagnetic-resonance and magnetic-circular-dichroism spectroscopy. The Biochemical Journal. 193: 699-708. PMID 6272717 DOI: 10.1042/Bj1930699 |
0.394 |
|
| 1982 |
Thomson AJ, Johnson MK, Greenwood C, Gooding PE. A study of the magnetic properties of haem a3 in cytochrome c oxidase by using magnetic-circular-dichroism spectroscopy. The Biochemical Journal. 193: 687-97. PMID 6272716 DOI: 10.1042/Bj1930687 |
0.412 |
|
| 1982 |
Brittain T, Greenwood C, Barber D. A characterization of ferric sulphaemoglobin Biochimica Et Biophysica Acta. 705: 26-32. DOI: 10.1016/0167-4838(82)90331-4 |
0.363 |
|
| 1982 |
Eglinton DG, Barber D, Thomson AJ, Greenwood C, Segal AW. Studies of cyanide binding to myeloperoxidase by electron paramagnetic resonance and magnetic circular dichroism spectroscopies Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 703: 187-195. DOI: 10.1016/0167-4838(82)90047-4 |
0.358 |
|
| 1982 |
Brittain T, Greenwood C, Springall J, Thomson A. The nature of ferrous haem protein complexes prepared by photolysis Biochimica Et Biophysica Acta (Bba) - Protein Structure and Molecular Enzymology. 703: 117-128. DOI: 10.1016/0167-4838(82)90039-5 |
0.329 |
|
| 1981 |
Edgerton ME, Moore TA, Greenwood C. Investigations into the effect of acid on the spectral and kinetic properties of purple membrane from Halobacterium halobium. The Biochemical Journal. 189: 413-20. PMID 7213336 DOI: 10.1042/Bj1890413 |
0.328 |
|
| 1981 |
Eglinton DG, Johnson MK, Thomson AJ, Gooding PE, Greenwood C. Near-infrared magnetic and natural circular dichroism of cytochrome c oxidase. The Biochemical Journal. 191: 319-31. PMID 6263244 DOI: 10.1042/Bj1910319 |
0.415 |
|
| 1981 |
Walsh TA, Johnson MK, Barber D, Thomson AJ, Greenwood C. Studies on heme d1 extracted from Pseudomonas aeruginosa nitrite reductase Journal of Inorganic Biochemistry. 14: 15-31. PMID 6260897 DOI: 10.1016/S0162-0134(00)80011-2 |
0.333 |
|
| 1981 |
Walsh TA, Johnson MK, Thomson AJ, Barber D, Greenwood C. The characterization and magnetic properties of the azide and imidazole derivatives of Pseudomonas nitrite reductase Journal of Inorganic Biochemistry. 14: 1-14. PMID 6260896 DOI: 10.1016/S0162-0134(00)80010-0 |
0.43 |
|
| 1980 |
Johnson MK, Thomson AJ, Walsh TA, Barber D, Greenwood C. Electron paramagnetic resonance studies on Pseudomonas nitrosyl nitrite reductase. Evidence for multiple species in the electron paramagnetic resonance spectra of nitrosyl haemoproteins Biochemical Journal. 189: 285-294. PMID 6257232 DOI: 10.1042/Bj1890285 |
0.389 |
|
| 1979 |
Walsh TA, Johnson MK, Greenwood C, Barber D, Springall JP, Thomson AJ. Some magnetic properties of Pseudomonas cytochrome oxidase Biochemical Journal. 177: 29-39. PMID 218561 DOI: 10.1042/Bj1770029 |
0.45 |
|
| 1979 |
Silvestrini MC, Colosimo A, Brunori M, Walsh TA, Barber D, Greenwood C. A re-evaluation of some basic structural and functional properties of Pseudomonas cytochrome oxidase Biochemical Journal. 183: 701-709. PMID 44192 DOI: 10.1042/Bj1830701 |
0.419 |
|
| 1978 |
Brittain T, Greenwood C, Springall JP, Thomson AJ. Magnetic-circular-dichroism studies of haem a and its derivatives. The Biochemical Journal. 173: 411-7. PMID 697728 DOI: 10.1042/Bj1730411 |
0.425 |
|
| 1978 |
Barber D, Parr SR, Greenwood C. The oxidation of Pseudomonas cytochrome c-551 oxidase by potassium ferricyanide. Biochemical Journal. 173: 681-690. PMID 212017 DOI: 10.1042/Bj1730681 |
0.399 |
|
| 1978 |
Greenwood C, Barber D, Parr SR, Antonini E, Brunori M, Colosimo A. The reaction of Pseudomonas aeruginosa cytochrome c-551 oxidase with oxygen. Biochemical Journal. 173: 11-17. PMID 210764 DOI: 10.1042/Bj1730011 |
0.444 |
|
| 1978 |
Barber D, Parr SR, Greenwood C. The reactions of Pseudomonas cytochrome c-551 oxidase with potassium cyanide Biochemical Journal. 175: 239-249. PMID 32876 DOI: 10.1042/Bj1750239 |
0.459 |
|
| 1978 |
Moore TA, Edgerton ME, Parr G, Greenwood C, Perham RN. Studies of an acid-induced species of purple membrane from Halobacterium halobium. The Biochemical Journal. 171: 469-76. PMID 26337 DOI: 10.1042/Bj1710469 |
0.311 |
|
| 1977 |
Parr SR, Barber D, Greenwood C, Brunori M. The electron-transfer reaction between azurin and the cytochrome c oxidase from Pseudomonas aeruginosa Biochemical Journal. 167: 447-455. PMID 202254 DOI: 10.1042/Bj1670447 |
0.435 |
|
| 1977 |
Greenwood C, Brittain T, Brunori M, Wilson MT. Chromous ion reduction of mammalian cytochrome oxidase and some of its derivatives. The Biochemical Journal. 165: 413-6. PMID 200223 DOI: 10.1042/Bj1650413 |
0.378 |
|
| 1977 |
Thomson AJ, Brittain T, Greenwood C, Springall JP. Variable-temperature magnetic-circular-dichroism spectra of cytochrome c oxidase and its derivatives. The Biochemical Journal. 165: 327-36. PMID 200221 DOI: 10.1042/Bj1650327 |
0.405 |
|
| 1977 |
Antonini E, Brunori M, Colosimo A, Greenwood C, Wilson MT. Oxygen "pulsed" cytochrome c oxidase: functional properties and catalytic relevance Proceedings of the National Academy of Sciences of the United States of America. 74: 3128-3132. PMID 198771 DOI: 10.1073/Pnas.74.8.3128 |
0.551 |
|
| 1977 |
Barber D, Parr SR, Greenwood C. The reduction of Pseudomonas cytochrome c551 oxidase by chromous ions. Biochemical Journal. 163: 629-632. PMID 195577 DOI: 10.1042/Bj1630629 |
0.413 |
|
| 1977 |
Brittain T, Springall J, Greenwood C, Thomson AJ. Low-temperature studies on mixed-valence cytochrome oxidase by using magnetic circular dichroism. The Biochemical Journal. 159: 811-3. PMID 188413 DOI: 10.1042/Bj1590811 |
0.312 |
|
| 1976 |
Greenwood C, Brittain T. Studies on partially reduced mammalian cytochrome oxidase reactions with ferrocytochrome c. The Biochemical Journal. 157: 591-8. PMID 186026 DOI: 10.1042/BJ1570591 |
0.345 |
|
| 1976 |
Barber D, Parr SR, Greenwood C. Some spectral and steady-state kinetic properties of Pseudomonas cytochrome oxidase. Biochemical Journal. 157: 431-438. PMID 183751 DOI: 10.1042/Bj1570431 |
0.413 |
|
| 1976 |
Parr SR, Barber D, Greenwood C. A purification procedure for the soluble cytochrome oxidase and some other respiratory proteins from Pseudomonas aeruginosa. Biochemical Journal. 157: 423-430. PMID 183750 DOI: 10.1042/Bj1570423 |
0.342 |
|
| 1976 |
Thomson AJ, Brittain T, Greenwood C, Springall J. Determination of the heme spin states in cytochrome c oxidase using magnetic circular dichroism. Febs Letters. 67: 94-8. PMID 182549 DOI: 10.1016/0014-5793(76)80877-0 |
0.411 |
|
| 1976 |
Brittain T, Greenwood C. Kinetic studies on the binding of cyanide to oxygenated cytochrome c oxidase. The Biochemical Journal. 155: 453-5. PMID 180986 DOI: 10.1042/BJ1550453 |
0.302 |
|
| 1976 |
Moore TA, Greenwood C. A method for investigating the effect of temperature on the 695 nm band of insoluble cytochrome c. The Biochemical Journal. 149: 169-77. PMID 172068 DOI: 10.1042/Bj1490169 |
0.351 |
|
| 1976 |
Greenwood C, Moore TA. An investigation of protein conformation of cytochrome c by using cytochrome c insolubilized on to agarose gel. The Biochemical Journal. 153: 159-63. PMID 6001 DOI: 10.1042/Bj1530159 |
0.411 |
|
| 1975 |
Brittain T, Greenwood C. Kinetic studies on mammalian cytochrome c modified with 2-hydroxy-5-hydroxy-5-nitrobenzyl bromide. The Biochemical Journal. 149: 179-85. PMID 242320 DOI: 10.1042/Bj1490179 |
0.313 |
|
| 1975 |
Moore TA, Greenwood C, Wilson MT. Ligand binding to ferrocytochrome c at high pH Biochemical Journal. 147: 335-341. PMID 241325 DOI: 10.1042/Bj1470335 |
0.407 |
|
| 1975 |
Brittain T, Greenwood C. A comparative study of some kinetic and spectral properties of guanidinated and native cytochrome c. The Biochemical Journal. 147: 175-7. PMID 239700 DOI: 10.1042/Bj1470175 |
0.398 |
|
| 1975 |
Gore MG, Greenwood C. Studies on the binary and ternary complexes formed by a Neurospora glutamate dehydrogenase and its substrates. Biochemical and Biophysical Research Communications. 62: 997-1002. PMID 235266 DOI: 10.1016/0006-291X(75)90421-0 |
0.324 |
|
| 1975 |
Parr SR, Wilson MT, Greenwood C. The reaction of Pseudomonas aeruginosa cytochrome c oxidase with carbon monoxide Biochemical Journal. 151: 51-59. PMID 174556 DOI: 10.1042/Bj1510051 |
0.371 |
|
| 1975 |
Brunori M, Parr SR, Greenwood C, Wilson MT. A temperature jump study of the reaction between azurin and cytochrome c oxidase from Pseudomonas aeruginosa Biochemical Journal. 151: 185-188. PMID 174553 DOI: 10.1042/Bj1510185 |
0.412 |
|
| 1975 |
Brittain T, Greenwood C. Kinetic studies on (N-formyltryptophyl)cytochrome c. The Biochemical Journal. 149: 713-7. PMID 173295 DOI: 10.1042/Bj1490713 |
0.373 |
|
| 1975 |
Wilson MT, Greenwood C, Brunori M, Antonini E. Kinetic studies on the reaction between cytochrome c oxidase and ferrocytochrome c Biochemical Journal. 147: 145-153. PMID 168879 DOI: 10.1042/Bj1470145 |
0.447 |
|
| 1975 |
Wilson MT, Greenwood C, Brunori M, Antonini E. Electron transfer between azurin and cytochrome c 551 from Pseudomonas aeruginosa Biochemical Journal. 145: 449-457. PMID 168867 DOI: 10.1042/Bj1450449 |
0.388 |
|
| 1975 |
Gore MG, Greenwood C. Regulatory properties of reduced nicotinamide-adenine dinucleotide phosphate on a glutamate dehydrogenase from Neurospora crassa International Journal of Biochemistry. 6: 829-833. DOI: 10.1016/0020-711X(75)90099-3 |
0.35 |
|
| 1974 |
Parr SR, Wilson MT, Greenwood C. The reaction of Pseudomonas aeruginosa cytochrome c oxidase with sodium metabisulphite Biochemical Journal. 139: 273-276. PMID 4377097 DOI: 10.1042/Bj1390273 |
0.561 |
|
| 1974 |
Brittain T, Wilson MT, Greenwood C. The reduction of carboxymethyl-cytochrome c by chromous ions. The Biochemical Journal. 141: 455-61. PMID 4375979 DOI: 10.1042/Bj1410455 |
0.454 |
|
| 1974 |
Dupre S, Brunori M, Wilson MT, Greenwood C. Kinetics of carbon monoxide binding and electron transfer by cytochrome c polymers Biochemical Journal. 141: 299-304. PMID 4375972 DOI: 10.1042/Bj1410299 |
0.536 |
|
| 1974 |
Greenwood C, Wilson MT, Brunori M. Studies on partially reduced mammalian cytochrome oxidase: reactions with carbon monoxide and oxygen Biochemical Journal. 137: 205-215. PMID 4363109 DOI: 10.1042/Bj1370205 |
0.401 |
|
| 1974 |
Brunori M, Greenwood C, Wilson MT. A temperature jump study of the reaction between azurin and cytochrome c 551 from Pseudomonas aeruginosa Biochemical Journal. 137: 113-116. PMID 4362494 DOI: 10.1042/Bj1370113 |
0.385 |
|
| 1974 |
Brittain T, Greenwood C. Preparation and some Properties of Mammalian Cytochrome c Modified with 2-Hydroxy-5-nitrobenzyl Bromide Biochemical Society Transactions. 2: 990-992. DOI: 10.1042/Bst0020990 |
0.374 |
|
| 1973 |
Antonini E, Brunori M, Greenwood C, Wilson MT. Kinetic Studies on Mammalian Cytochrome c Oxidase Biochemical Society Transactions. 1: 34-35. DOI: 10.1042/Bst0010034 |
0.547 |
|
| 1971 |
Greenwood C, Wilson MT. Studies on ferricytochrome c. I. Effect of pH, ionic strength and protein denaturants on the spectra of ferricytochrome c European Journal of Biochemistry. 22: 5-10. PMID 5099216 DOI: 10.1111/J.1432-1033.1971.Tb01507.X |
0.496 |
|
| 1971 |
Wilson MT, Greenwood C. Studies on ferricytochrome c. 2. A correlation between reducibility and the possession of the 695mm absorption band of ferricytochrome c European Journal of Biochemistry. 22: 11-18. PMID 5099209 DOI: 10.1111/J.1432-1033.1971.Tb01508.X |
0.507 |
|
| 1971 |
Antonini E, Brunori M, Greenwood C, Malmström BG, Rotilio GC. The interaction of cyanide with cytochrome oxidase. European Journal of Biochemistry / Febs. 23: 396-400. PMID 4333368 DOI: 10.1111/J.1432-1033.1971.Tb01633.X |
0.457 |
|
| 1971 |
Greenwood C, Agrò AF, Guerrieri P, Avigliano L, MondovÍ B, Antonini E. Electron‐Transfer Reactions between Redox Proteins from a Bacterium (Pseudomonas fluorescens) and Mammalian‐Heart Muscle Febs Journal. 23: 321-327. PMID 4333365 DOI: 10.1111/J.1432-1033.1971.Tb01624.X |
0.412 |
|
| 1970 |
Antonini E, Brunori M, Greenwood C, Malmström BG. Catalytic mechanism of cytochrome oxidase. Nature. 228: 936-7. PMID 4320510 DOI: 10.1038/228936A0 |
0.313 |
|
| 1965 |
GIBSON QH, HASTINGS JW, GREENWOOD C. ON THE MOLECULAR MECHANISM OF BIOLUMINESCENCE, II. LIGHT-INDUCED Proceedings of the National Academy of Sciences of the United States Of. 53: 187-195. PMID 14283197 DOI: 10.1073/Pnas.53.1.187 |
0.407 |
|
| 1965 |
Hastings JW, Gibson QH, Greenwood C. EVIDENCE FOR HIGH ENERGY STORAGE INTERMEDIATES IN BIOLUMINESCENCE Photochemistry and Photobiology. 4: 1227-1241. DOI: 10.1111/J.1751-1097.1965.Tb09309.X |
0.471 |
|
| 1964 |
HASTINGS JW, GIBSON QH, GREENWOOD C. ON THE MOLECULAR MECHANISM OF BIOLUMINESCENCE. I. THE ROLE OF Proceedings of the National Academy of Sciences of the United States Of. 52: 1529-1535. PMID 14243528 DOI: 10.1073/pnas.52.6.1529 |
0.404 |
|
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