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William A. Cramer
Researcher at Purdue University
Publications - 243
Citations - 11729
William A. Cramer is an academic researcher from Purdue University. The author has contributed to research in topics: Cytochrome b6f complex & Colicin. The author has an hindex of 61, co-authored 239 publications receiving 11229 citations. Previous affiliations of William A. Cramer include University of Amsterdam & Albert Einstein College of Medicine.
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Journal ArticleDOI
Structure of the Cytochrome b6f Complex of Oxygenic Photosynthesis: Tuning the Cavity
TL;DR: The dimeric b6f complex from the thermophilic cyanobacterium Mastigocladus laminosus reveals a large quinone exchange cavity, stabilized by lipid, in which plastoquinone, a quin one-analog inhibitor, and a novel heme are bound.
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Sequence homology and structural similarity between cytochrome b of mitochondrial complex III and the chloroplast b6-f complex: position of the cytochrome b hemes in the membrane.
TL;DR: Calculation of the distribution of hydrophobic residues with a "hydropathy" function that is conserved in this family of proteins implies that the membrane-folding pattern of the 42-kilodalton (kDa) mitochondrial cytochromes involves 8-9 membrane-spanning domains.
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Crystal structure of chloroplast cytochrome freveals a novel cytochrome fold and unexpected heme ligation
TL;DR: The structure of cy tochrome f allows prediction of the approximate docking site of plastocyanin and should allow systematic studies of the mechanism of intra- and inter-protein electron transfer between the cytochrome heme and plastOCyanin copper, which are approximately isopotential.
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Structure-function of the channel-forming colicins.
William A. Cramer,J. B. Heymann,Sharon L. Schendel,B.N. Deriy,Fredric S. Cohen,P. Elkins,Cynthia V. Stauffacher +6 more
TL;DR: Unique aspects of the colicin channel system are the involvement of protein import in the gating process, the existence of multiple open and closed states, and the existence and action of an immunity protein that involves specific intramembrane helix-helix interactions with transmembrane helices of the channel-forming domains.
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SOME NEW STRUCTURAL ASPECTS AND OLD CONTROVERSIES CONCERNING THE CYTOCHROME b6f COMPLEX OF OXYGENIC PHOTOSYNTHESIS.
William A. Cramer,G. M. Soriano,M. Ponomarev,D. Huang,Huamin Zhang,Sergio E. Martinez,Janet L. Smith +6 more
TL;DR: An unusual electron transfer event, the oxidant-induced reduction of a significant fraction of the p (lumen)-side cytochrome b heme by plastosemiquinone indicates that the electron transfer pathway in the b6f complex can be described by a version of the Q-cycle mechanism.