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Article

Direct electrochemistry and EPR spectroscopy of spinach ferredoxin mutants with modified electron transfer properties.

FEBS letters - 17 Jul 1995

Aliverti A, Hagen W R, Zanetti G

Abstract excerpt

Mutations of the conserved residue Glu-92 to lysine, glutamine, and alanine have been performed in the recombinant ferredoxin I of spinach leaves. The purified ferredoxin mutants were found twice as active with respect to wild-type protein in the NADPH-cytochrome c reductase reaction catalyzed by ferredoxin-NADP+ reductase in the presence of ferredoxin. Cyclic voltammetry and EPR measurements showed that the...

Topics

Electric Conductivity
Electron Spin Resonance Spectroscopy
Electron Transport
Escherichia coli
Ferredoxins
Glutamic Acid
Mutation
NADPH-Ferrihemoprotein Reductase
Recombinant Fusion Proteins
Spinacia oleracea

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Identifiers

PMID: 7628609
DOI: 10.1016/0014-5793(95)00648-s

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-7628609-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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