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PMID: 3016897 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, Non-P.H.S.

Long-range electron transfer in heme proteins.

Science (New York, N.Y.) ·Vol. 233 ·No. 4767 ·1986-08-29 ·Pages 948-52

Mayo SL, Ellis WR, Crutchley RJ, Gray HB

Abstract

Kinetic experiments have conclusively shown that electron transfer can take place over large distances (greater than 10 angstroms) through protein interiors. Current research focuses on the elucidation of the factors that determine the rates of long-range electron-transfer reactions in modified proteins and protein complexes. Factors receiving experimental and theoretical attention include the donor-acceptor distance, changes in geometry of the donor and acceptor upon electron transfer, and the thermodynamic driving force. Recent experimental work on heme proteins indicates that the electron-transfer rate falls off exponentially with donor-acceptor distance at long range. The rate is greatly enhanced in proteins in which the structural changes accompanying electron transfer are very small.

MeSH Terms
Animals Cytochrome c Group/metabolism Electron Transport Hemeproteins/metabolism Horses/metabolism Metalloporphyrins/metabolism Myoglobin/metabolism Pseudomonas aeruginosa/metabolism Thermodynamics
Chemicals
Cytochrome c Group Hemeproteins Metalloporphyrins Myoglobin zinc hematoporphyrin
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Mayo S L
Ellis W R
Crutchley R J
Gray H B
Article Info
Journal
Science (New York, N.Y.)
Abbr.
Science
ISSN
0036-8075
Published
1986-08-29
Pages
948-52
Language
English
Region
United States
NLM ID
0404511
Subset
IM
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