Published November 25, 1983
| public
Journal Article
Heme-Heme Orientation and Electron Transfer Kinetic Behavior of Multisite Oxidation-Reduction Enzymes
Abstract
Analysis of the polarized single-crystal absorption spectra of cytochrome cd1 of Pseudomonas aeruginosa shows that the heme c and heme d_1 groups in each subunit are oriented perpendicularly to each other in both oxidized and reduced forms of the enzyme. These results, together with those of previous kinetic studies, indicate that a perpendicular heme-heme orientation may be an important factor in specifying kinetically slow steps in a sequential series of electron transfer reactions.
Additional Information
© 1983 American Association for the Advancement of Science. 13 June 1983; accepted 21 September 1983. We thank Dr. T. Takano for providing crystals of cytochrome cd_1. Supported by NSF grant PCM 77-13479 (M.W.M.), American Heart Association grant-in-aid 77378 (M.W.M.), NSF grant CHE 82-18502 (H.B.G.), and NIH training grant 1-T32-HD-07009 (S.A.S.). This is contribution No. 6774 from the Arthur Amos Noyes Laboratory.Additional details
- Eprint ID
- 54522
- Resolver ID
- CaltechAUTHORS:20150209-090647293
- PCM 77-13479
- NSF
- 77378
- American Heart Association
- CHE 82-18502
- NSF
- 1-T32-HD-07009
- NIH
- Created
-
2015-02-09Created from EPrint's datestamp field
- Updated
-
2021-11-10Created from EPrint's last_modified field
- Other Numbering System Name
- Caltech Arthur Amos Noyes Laboratory
- Other Numbering System Identifier
- 6774