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Variation in the Formal Reduction Potential of an (2FE-2S) Iron-Sulfur Protein and its Mutants

Published

Author(s)

V L. Vilker, Vytautas Reipa, Marcia J. Holden, M P. Mayhew

Abstract

We have been pursuing the detailed pathway by which cytochrome P450cam (CYP101) transfers electrons through a three diffusible protein subunit system, and how this system might be engineered to eliminate nonessential subunits and the costly NADH cofactor. One of these subunit proteins, putidaredoxin (Pdx), is an 11.6 kDa [Fe2S2] redox protein that transfers two electrons in two separate steps from the flavin containing putidaredoxin reductase (PdR) to the heme protein, cytochrome CYP101 in the P450cam catalytic cycle. It has recently come to light, through NMR measurements, that there can be appreciable differences in the conformational dynamics between the reduced and oxidized states of Pdx, which in turn, effects its interaction with its redox partners, and metal oxide electrodes. In the current investigation, we describe our efforts to measure the formal potential (E0') of wild-type putidaredoxin and selected mutants, as a function of temperature with the expectation of learning more about the behavior of this protein as a function of its oxidation state.
Proceedings Title
Manuael M Balzer; New Directions in Organic Electrochemistry, International Symposium | 4th | | Electrochemical Society
Volume
No. 15
Conference Dates
May 1, 2000
Conference Location
Toronto, CA
Conference Title
Electrochemical Society

Keywords

iron-sulfur protein, P450, putidaredoxin, redox potential, spectroelectrochemistry

Citation

Vilker, V. , Reipa, V. , Holden, M. and Mayhew, M. (2000), Variation in the Formal Reduction Potential of an (2FE-2S) Iron-Sulfur Protein and its Mutants, Manuael M Balzer; New Directions in Organic Electrochemistry, International Symposium | 4th | | Electrochemical Society, Toronto, CA (Accessed June 25, 2024)

Issues

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Created May 1, 2000, Updated February 17, 2017