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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
48
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pubmed:dateCreated |
1994-1-6
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pubmed:abstractText |
Kinetics of flash-induced electron transfer from the soluble cytochrome c2 to the primary donor (P) of the reaction center purified from the purple bacterium Rhodobacter sphaeroides R-26 were investigated by time-resolved absorption spectroscopy. Re-reduction of P+ induced by a laser pulse was measured at 1283 nm both in isolated reaction centers and in reconstituted proteoliposomes reproducing the lipid composition of the native membrane. The effects of temperature (230-300 K) and of the cytochrome c2/reaction center stoichiometry were examined. At room temperature, over a wide range of cytochrome c2 to reaction center molar ratios, the biphasic kinetics of cytochrome c2 oxidation in the microsecond-to-millisecond time scale could be accurately described by a minimum reaction scheme which includes a second-order collisional process (k = 1.4 x 10(9) M-1 s-1 and k = 2.4 x 10(9) M-1 s-1 in isolated and reconstituted reaction centers, respectively) and a first-order intracomplex electron donation (t1/2 = 590 +/- 110 ns in isolated reaction centers; t1/2 = 930 +/- 140 ns in proteoliposomes). At cytochrome c2 to reaction center molar ratios exceeding 5, the monomolecular process almost completely accounts for P+ re-reduction. At lower stoichiometries, the relative contribution of the two parallel reaction pathways is modulated by a single binding equilibrium between cytochrome c2 and reaction centers, yielding a binding constant of 3.5 x 10(5) M-1 in both systems.(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/Cytochrome c Group,
http://linkedlifedata.com/resource/pubmed/chemical/Cytochromes c2,
http://linkedlifedata.com/resource/pubmed/chemical/Photosynthetic Reaction Center...,
http://linkedlifedata.com/resource/pubmed/chemical/Proteolipids,
http://linkedlifedata.com/resource/pubmed/chemical/proteoliposomes
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
7
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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 |
13245-53
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:8241180-Cytochrome c Group,
pubmed-meshheading:8241180-Cytochromes c2,
pubmed-meshheading:8241180-Electron Transport,
pubmed-meshheading:8241180-Kinetics,
pubmed-meshheading:8241180-Oxidation-Reduction,
pubmed-meshheading:8241180-Photosynthesis,
pubmed-meshheading:8241180-Photosynthetic Reaction Center Complex Proteins,
pubmed-meshheading:8241180-Proteolipids,
pubmed-meshheading:8241180-Rhodobacter sphaeroides,
pubmed-meshheading:8241180-Temperature,
pubmed-meshheading:8241180-Thermodynamics
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pubmed:year |
1993
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pubmed:articleTitle |
Electron transfer from cytochrome c2 to the primary donor of Rhodobacter sphaeroides reaction centers. A temperature dependence study.
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pubmed:affiliation |
Dipartimento di Biologia, Università di Bologna, Italy.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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