Ferredoxin/flavoprotein-linked Pathway for the Reduction of Thioredoxin

Overview

Journal Proc Natl Acad Sci U S A

Specialty Science

Date 1983 Jun 1

PMID 6574505

Citations 13

Authors

K E Hammel

K L Cornwell

B B Buchanan

Affiliations

Soon will be listed here.

Abstract

Thioredoxins are small redox proteins, alternating between the S-S (oxidized) and SH (reduced) states, that function in a number of important biochemical processes, including DNA synthesis, DNA replication, and enzyme regulation. Reduced ferredoxin is known to serve as the source of reducing power for the reduction of thioredoxins only in photosynthetic cells that evolve oxygen. In all other organisms, the source of hydrogen (electrons) for thioredoxin reduction is considered to be NADPH. We now report evidence that Clostridium pasteurianum, an anaerobic bacterium normally living in the soil unexposed to light, resembles photosynthetic cells in that it uses reduced ferredoxin as the reductant for thioredoxin. Moreover, the transfer of electrons from reduced ferredoxin to thioredoxin is catalyzed by a flavoprotein enzyme that has not been detected in other organisms. Our results reveal the existence of a pathway for the reduction of thioredoxin in which ferredoxin, reduced fermentatively either by molecular hydrogen or by a carbon substrate, provides the reducing power for the flavoprotein enzyme ferredoxin-thioredoxin reductase, which in turn reduces thioredoxin.

Citing Articles

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Structural and Biochemical Characterization of Thioredoxin-2 from .

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Atomic Force Microscopy to Elicit Conformational Transitions of Ferredoxin-Dependent Flavin Thioredoxin Reductases.

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Unexpected diversity of ferredoxin-dependent thioredoxin reductases in cyanobacteria.

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