Interaction between cytochrome c2 and reaction centers from purple bacteria

S. Wang, X. Li, J. C. Williams, James Paul Allen, P. Mathis

Research output: Contribution to journalArticle

18 Citations (Scopus)

Abstract

The kinetics of electron transfer of c2 tochrome c2 from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodospirillum centenum to reaction centers from Rb. sphaeroides and Rb. capsulatus have been measured. Observed in the kinetics of decay of the oxidized donor are a rapid first-order rate and one or more slower rates that are due to diffusion-limited complex formation. For reaction centers from Rb. sphaeroides, the fast component had time constants of 1.0 and 0.5 μs for cytochrome c2 from Rb. sphaeroides and Rb. capsulatus, respectively, but only a slow component was observed for cytochrome c2 from Rs. centenum. For reaction centers from Rb. capsulatus, the kinetics from all three cytochromes had a fast component with time constants of 1.0, 0.7, and 1.9 μS for cytochrome c2 from Rb. sphaeroides, Rb. capsulatus, and Rs. centenum, respectively, although the dissociation constant for cytochrome c2 from Rs. centenum was approximately 20 times larger than that of the other cytochromes. The observation of the fast component for cytochrome c2 from Rs. centenum in reaction centers from Rb. capsulatus but not Rb. sphaeroides demonstrates that the binding interactions for the two reaction centers differ, and the involvement of amino acid residues in the binding is discussed. The kinetics of electron transfer from cytochrome c2 to reaction centers of Rb. sphaeroides from wild type and three mutant strains that have altered carboxyl-terminal regions of the M subunit of the reaction center have also been measured. For cytochrome c2 from Rb. sphaeroides, the kinetics are very similar between the mutants and wild type. In contrast, for cytochrome c2 from Rb. capsulatus, the dissociation constants vary from 2.4 to 18 μM in the mutants compared to 6.3 μM for wild type. A greater involvement for the M carboxyl region in the binding of the cytochrome c2 from Rb. capsulatus is proposed.

Original languageEnglish
Pages (from-to)8306-8312
Number of pages7
JournalBiochemistry
Volume33
Issue number27
Publication statusPublished - 1994

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Cytochromes c2
Proteobacteria
Kinetics
Cytochromes
Rhodospirillum centenum
Electrons
Rhodobacter capsulatus
Rhodobacter sphaeroides
Observation

ASJC Scopus subject areas

  • Biochemistry

Cite this

Wang, S., Li, X., Williams, J. C., Allen, J. P., & Mathis, P. (1994). Interaction between cytochrome c2 and reaction centers from purple bacteria. Biochemistry, 33(27), 8306-8312.

Interaction between cytochrome c2 and reaction centers from purple bacteria. / Wang, S.; Li, X.; Williams, J. C.; Allen, James Paul; Mathis, P.

In: Biochemistry, Vol. 33, No. 27, 1994, p. 8306-8312.

Research output: Contribution to journalArticle

Wang, S, Li, X, Williams, JC, Allen, JP & Mathis, P 1994, 'Interaction between cytochrome c2 and reaction centers from purple bacteria', Biochemistry, vol. 33, no. 27, pp. 8306-8312.
Wang, S. ; Li, X. ; Williams, J. C. ; Allen, James Paul ; Mathis, P. / Interaction between cytochrome c2 and reaction centers from purple bacteria. In: Biochemistry. 1994 ; Vol. 33, No. 27. pp. 8306-8312.
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N2 - The kinetics of electron transfer of c2 tochrome c2 from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodospirillum centenum to reaction centers from Rb. sphaeroides and Rb. capsulatus have been measured. Observed in the kinetics of decay of the oxidized donor are a rapid first-order rate and one or more slower rates that are due to diffusion-limited complex formation. For reaction centers from Rb. sphaeroides, the fast component had time constants of 1.0 and 0.5 μs for cytochrome c2 from Rb. sphaeroides and Rb. capsulatus, respectively, but only a slow component was observed for cytochrome c2 from Rs. centenum. For reaction centers from Rb. capsulatus, the kinetics from all three cytochromes had a fast component with time constants of 1.0, 0.7, and 1.9 μS for cytochrome c2 from Rb. sphaeroides, Rb. capsulatus, and Rs. centenum, respectively, although the dissociation constant for cytochrome c2 from Rs. centenum was approximately 20 times larger than that of the other cytochromes. The observation of the fast component for cytochrome c2 from Rs. centenum in reaction centers from Rb. capsulatus but not Rb. sphaeroides demonstrates that the binding interactions for the two reaction centers differ, and the involvement of amino acid residues in the binding is discussed. The kinetics of electron transfer from cytochrome c2 to reaction centers of Rb. sphaeroides from wild type and three mutant strains that have altered carboxyl-terminal regions of the M subunit of the reaction center have also been measured. For cytochrome c2 from Rb. sphaeroides, the kinetics are very similar between the mutants and wild type. In contrast, for cytochrome c2 from Rb. capsulatus, the dissociation constants vary from 2.4 to 18 μM in the mutants compared to 6.3 μM for wild type. A greater involvement for the M carboxyl region in the binding of the cytochrome c2 from Rb. capsulatus is proposed.

AB - The kinetics of electron transfer of c2 tochrome c2 from Rhodobacter sphaeroides, Rhodobacter capsulatus, and Rhodospirillum centenum to reaction centers from Rb. sphaeroides and Rb. capsulatus have been measured. Observed in the kinetics of decay of the oxidized donor are a rapid first-order rate and one or more slower rates that are due to diffusion-limited complex formation. For reaction centers from Rb. sphaeroides, the fast component had time constants of 1.0 and 0.5 μs for cytochrome c2 from Rb. sphaeroides and Rb. capsulatus, respectively, but only a slow component was observed for cytochrome c2 from Rs. centenum. For reaction centers from Rb. capsulatus, the kinetics from all three cytochromes had a fast component with time constants of 1.0, 0.7, and 1.9 μS for cytochrome c2 from Rb. sphaeroides, Rb. capsulatus, and Rs. centenum, respectively, although the dissociation constant for cytochrome c2 from Rs. centenum was approximately 20 times larger than that of the other cytochromes. The observation of the fast component for cytochrome c2 from Rs. centenum in reaction centers from Rb. capsulatus but not Rb. sphaeroides demonstrates that the binding interactions for the two reaction centers differ, and the involvement of amino acid residues in the binding is discussed. The kinetics of electron transfer from cytochrome c2 to reaction centers of Rb. sphaeroides from wild type and three mutant strains that have altered carboxyl-terminal regions of the M subunit of the reaction center have also been measured. For cytochrome c2 from Rb. sphaeroides, the kinetics are very similar between the mutants and wild type. In contrast, for cytochrome c2 from Rb. capsulatus, the dissociation constants vary from 2.4 to 18 μM in the mutants compared to 6.3 μM for wild type. A greater involvement for the M carboxyl region in the binding of the cytochrome c2 from Rb. capsulatus is proposed.

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