Literature DB >> 2985069

Binding of cytochrome c2 to the isolated reaction center of Rhodospirillum rubrum involves the "backside" of cytochrome c2.

R Rieder, V Wiemken, R Bachofen, H R Bosshard.   

Abstract

Lys 109, Lys 112 and Glu 1 of cytochrome c2 from Rhodospirillum rubrum G-9 are about 4-fold less reactive towards acetic anhydride when cytochrome c2 is bound to the isolated photosynthetic reaction center from the same organism. The three shielded residues are clustered together on the "backside" of cytochrome c2. This contrasts with mitochondrial cytochrome c where "frontside" lysines are protected by different physiological electron transfer partners.

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Year:  1985        PMID: 2985069     DOI: 10.1016/0006-291x(85)91653-5

Source DB:  PubMed          Journal:  Biochem Biophys Res Commun        ISSN: 0006-291X            Impact factor:   3.575


  2 in total

1.  Interaction of horse cytochrome c with the photosynthetic reaction center of Rhodospirillum rubrum.

Authors:  H R Bosshard; M Snozzi; R Bachofen
Journal:  J Bioenerg Biomembr       Date:  1987-08       Impact factor: 2.945

2.  Isolation of cytochrome bc 1 complexes from the photosynthetic bacteria Rhodopseudomonas viridis and Rhodospirillum rubrum.

Authors:  R M Wynn; D F Gaul; W K Choi; R W Shaw; D B Knaff
Journal:  Photosynth Res       Date:  1986-01       Impact factor: 3.573

  2 in total

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