The catalytic pathway of cytochrome P450cam at atomic resolution

Science

Volumn 287, Issue 5458, 2000, Pages 1615-1622

  Schlichting, Ilme ^a   Berendzen, Joel ^b   Chu, Kelvin ^b,g   Stock, Ann M ^c   Maves, Shelley A ^d   Benson, David E ^d   Sweet, Robert M ^e   Ringe, Dagmar ^f   Petsko, Gregory A ^f   Sligar, Stephen G ^a,d  

^a MAX PLANCK INSTITUTE OF MOLECULAR PHYSIOLOGY   (Germany)

^b LOS ALAMOS NATIONAL LABORATORY   (United States)

^c RUTGERS UNIVERSITY   (United States)

^d UNIVERSITY OF ILLINOIS AT URBANA CHAMPAIGN   (United States)

^e BROOKHAVEN NATIONAL LABORATORY   (United States)

^f BRANDEIS UNIVERSITY   (United States)

^g UNIVERSITY OF VERMONT   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CAMPHOR; CAMPHOR 5 MONOOXYGENASE; HYDROCARBON; OXYGEN; PROTON; WATER;

ARTICLE; CATALYST; CRYSTALLOGRAPHY; ELECTRON; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE COMPLEX; ENZYMOLOGY; HIGH TEMPERATURE; HYDROPHILICITY; HYDROXYLATION; PRIORITY JOURNAL; PSEUDOMONAS PUTIDA; RADIOLYSIS; WATER STRUCTURE;

CAMPHOR; CAMPHOR 5-MONOOXYGENASE; CATALYSIS; CRYSTALLIZATION; CRYSTALLOGRAPHY, X-RAY; ELECTRONS; FERRIC COMPOUNDS; FERROUS COMPOUNDS; HYDROGEN BONDING; HYDROXYLATION; LIGANDS; MODELS, MOLECULAR; MOLECULAR CONFORMATION; OXYGEN; PROTEIN CONFORMATION; PROTEIN STRUCTURE, SECONDARY; PROTONS; PSEUDOMONAS PUTIDA; WATER;

DRYOBALANOPS; PSEUDOMONAS; PSEUDOMONAS PUTIDA;

EID: 0034088779     PISSN: 00368075     EISSN: None     Source Type: Journal    
DOI: 10.1126/science.287.5458.1615     Document Type: Article

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68. The literature of cytochrome P450 is so vast, and so many people have made important contributions, that it is impossible in the space allowed to give even a representative set of references. We have tried to cite review articles whenever possible to provide links to the original papers. We apologize to those we have been unable to include. We gratefully acknowledge G. Holtermann for designing the pressure cell; M. Davies, N. C. Gerber, E. J. Mueller, and M. Vidakovic for supplying us with protein; C. Jung, G. Rosenbaum, and K. Scheffzek for discussions; and R. S. Goody, K. C. Holmes, and W. Kabsch for continuous support and encouragement. P. Ortiz de Montellano and J. A. Peterson provided useful advice. The referees made a number of very helpful suggestions that greatly improved the manuscript. We thank the Alexander von Humboldt Stiftung, the Human Frontiers Science Project, and the Richard und Anne Liese Leyendecker Stiftung for generous support and acknowledge the European Community biotech grant BIO2-CT942060 to I.S., NIH grants GM31756 and GM33775 to S.G.S, and GM26788 to G.A.P. and D.R. Beamline X12C is supported by the U.S. Department of Energy Offices of Health and Environmental Research and of Basic Energy Sciences, NIH, and NSF. The coordinates have been submitted to the PDB: 1d26, 1d24, 1d28, and 1d29 for the ferric, reduced, oxy, and oxyferryl complex, respectively.