» Articles » PMID: 20089857

Molecular Basis for Directional Electron Transfer

Overview
Journal J Biol Chem
Specialty Biochemistry
Date 2010 Jan 22
PMID 20089857
Citations 4
Authors
Affiliations
Soon will be listed here.
Abstract

Biological macromolecules involved in electron transfer reactions display chains of closely packed redox cofactors when long distances must be bridged. This is a consequence of the need to maintain a rate of transfer compatible with metabolic activity in the framework of the exponential decay of electron tunneling with distance. In this work intermolecular electron transfer was studied in kinetic experiments performed with the small tetraheme cytochrome from Shewanella oneidensis MR-1 and from Shewanella frigidimarina NCIMB400 using non-physiological redox partners. This choice allowed the effect of specific recognition and docking to be eliminated from the measured rates. The results were analyzed with a kinetic model that uses the extensive thermodynamic characterization of these proteins reported in the literature to discriminate the kinetic contribution of each heme to the overall rate of electron transfer. This analysis shows that, in this redox chain that spans 23 A, the kinetic properties of the individual hemes establish a functional specificity for each redox center. This functional specificity combined with the thermodynamic properties of these soluble proteins ensures directional electron flow within the cytochrome even outside of the context of a functioning respiratory chain.

Citing Articles

Biochemical and cellular characterization of the CISD3 protein: Molecular bases of cluster release and destabilizing effects of nitric oxide.

Grifagni D, Silva J, Querci L, Lepoivre M, Vallieres C, Louro R J Biol Chem. 2024; 300(3):105745.

PMID: 38354784 PMC: 10937110. DOI: 10.1016/j.jbc.2024.105745.


Modulation of the reactivity of multiheme cytochromes by site-directed mutagenesis: moving towards the optimization of microbial electrochemical technologies.

Alves A, Costa N, Tien M, Louro R, Paquete C J Biol Inorg Chem. 2016; 22(1):87-97.

PMID: 27817033 DOI: 10.1007/s00775-016-1409-0.


The Multicenter Aerobic Iron Respiratory Chain of Acidithiobacillus ferrooxidans Functions as an Ensemble with a Single Macroscopic Rate Constant.

Li T, Painter R, Ban B, Blake 2nd R J Biol Chem. 2015; 290(30):18293-303.

PMID: 26041781 PMC: 4513090. DOI: 10.1074/jbc.M115.657551.


Recent advances in bacterial heme protein biochemistry.

Mayfield J, Dehner C, DuBois J Curr Opin Chem Biol. 2011; 15(2):260-6.

PMID: 21339081 PMC: 3074008. DOI: 10.1016/j.cbpa.2011.02.002.

References
1.
McKenna C, Gutheil W, Song W . A method for preparing analytically pure sodium dithionite. Dithionite quality and observed nitrogenase-specific activities. Biochim Biophys Acta. 1991; 1075(1):109-17. DOI: 10.1016/0304-4165(91)90082-r. View

2.
Fredrickson J, Zachara J . Electron transfer at the microbe-mineral interface: a grand challenge in biogeochemistry. Geobiology. 2008; 6(3):245-53. DOI: 10.1111/j.1472-4669.2008.00146.x. View

3.
Tsapin A, Vandenberghe I, Nealson K, Scott J, Meyer T, Cusanovich M . Identification of a small tetraheme cytochrome c and a flavocytochrome c as two of the principal soluble cytochromes c in Shewanella oneidensis strain MR1. Appl Environ Microbiol. 2001; 67(7):3236-44. PMC: 93006. DOI: 10.1128/AEM.67.7.3236-3244.2001. View

4.
Gordon E, Pike A, Hill A, Cuthbertson P, Chapman S, Reid G . Identification and characterization of a novel cytochrome c(3) from Shewanella frigidimarina that is involved in Fe(III) respiration. Biochem J. 2000; 349(Pt 1):153-8. PMC: 1221132. DOI: 10.1042/0264-6021:3490153. View

5.
Hoffman B, Celis L, Cull D, Patel A, Seifert J, Wheeler K . Differential influence of dynamic processes on forward and reverse electron transfer across a protein-protein interface. Proc Natl Acad Sci U S A. 2005; 102(10):3564-9. PMC: 553314. DOI: 10.1073/pnas.0408767102. View