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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
32
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pubmed:dateCreated |
1993-9-16
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pubmed:abstractText |
In a previous paper we showed that the C51D mutant of PsaC contains a [3Fe-4S] cluster in the FA site and a [4Fe-4S] cluster in the FB site and that the C14D mutant contains an uncharacterized cluster in the FB site and a [4Fe-4S] cluster in the FA site [Zhao, J. D., Li, N., Warren, P. V., Golbeck, J. H., & Bryant, D. A. (1992) Biochemistry 31, 5093-5099]. In this paper we describe the electrochemical and electron spin resonance properties of the recombinant C14D and C51D holoproteins after in vitro reinsertion of the iron-sulfur clusters. Unbound PsaC shows no significant resonances in the oxidized state, but the unbound C14D and C51D mutant proteins show an intense set of resonances at g approximately 2.02 and 1.99 characteristic of an oxidized [3Fe-4S]1+/0 cluster. The Em' values for the [3Fe-4S]1+/0 clusters in C14D (FB*) and C51D (FA*) are -98 mV, and both represent one-electron transfers. After reduction with dithionite at pH 10.0, wild-type PsaC shows a broad set of resonances resulting from the superposition of FA- and FB- characterized by a low-field peak at an apparent g value of 2.051 and a high-field trough at an apparent g value of 1.898. The FB resonances in C51D were slightly narrower, with a low-field peak at an apparent g value of 2.039 and high-field trough at an apparent g value of 1.908.(ABSTRACT TRUNCATED AT 250 WORDS)
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Bacterial Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Iron-Sulfur Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Photosystem I Protein Complex,
http://linkedlifedata.com/resource/pubmed/chemical/photosystem I, psaB subunit
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pubmed:status |
MEDLINE
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pubmed:month |
Aug
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
17
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pubmed:volume |
32
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
8251-8
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8394132-Bacterial Proteins,
pubmed-meshheading:8394132-Cyanobacteria,
pubmed-meshheading:8394132-Electrochemistry,
pubmed-meshheading:8394132-Electron Spin Resonance Spectroscopy,
pubmed-meshheading:8394132-Escherichia coli,
pubmed-meshheading:8394132-Gene Expression,
pubmed-meshheading:8394132-Iron-Sulfur Proteins,
pubmed-meshheading:8394132-Membrane Proteins,
pubmed-meshheading:8394132-Microwaves,
pubmed-meshheading:8394132-Mutagenesis,
pubmed-meshheading:8394132-Oxidation-Reduction,
pubmed-meshheading:8394132-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:8394132-Photosystem I Protein Complex,
pubmed-meshheading:8394132-Plasmids,
pubmed-meshheading:8394132-Temperature
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pubmed:year |
1993
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pubmed:articleTitle |
Characterization of the [3Fe-4S] and [4Fe-4S] clusters in unbound PsaC mutants C14D and C51D. Midpoint potentials of the single [4Fe-4S] clusters are identical to FA and FB in bound PsaC of photosystem I.
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pubmed:affiliation |
Department of Biochemistry, University of Nebraska, Lincoln 68583-0718.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, Non-P.H.S.
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