The two last overviews by Colin Allen Wraight (1945–2014) on energy conversion in photosynthetic bacteria
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Colin Allen Wraight (1945–2014) was a well-known biophysicist and biochemist of our times—formerly Professor of Biochemistry, Biophysics and Plant Biology, and Head of the Department of Biochemistry, University of Illinois at Urbana-Champaign, Urbana, IL, USA. (See a detailed Tribute to him by Govindjee et al., Photosynth Res, 2015.) During the latter part of his life, Colin had (1) given an excellent lecture in 2008 on the overall topic of the molecular mechanisms in biological energy conversion, focusing on how an ubiquinone is reduced to ubiquinol at the so-called “two electron gate”, and (2) presented a review poster on the design features of long distance proton transport in biological systems, with focus on photosynthetic bacteria (a pdf file of the original is available from one of us, Govindjee). We present here for historical purpose, a complete transcript of his 2008 lecture and his 2013 poster, which have been annotated and expanded by the authors of this paper. The major theme is: electron and proton transfer in biological systems, with emphasis on bacterial reaction centers. The figures, some of which were prepared by us, are presented in sequence for both the lecture and the poster. A common bibliography is provided at the end of the paper, which is divided into two parts: (I) The Lecture; and (II) The Poster.
KeywordsBioenergetics Purple bacteria Reaction center Ubiquinones Light induced electron and proton transfer Two Electron Gate
We are thankful to Debora Ann Lanter of the School of Integrative Biology, University of Illinois at Urbana-Champaign (UIUC) for transcribing Colin Wraight’s lecture that we have annotated, edited and presented here. Further, we are grateful to Joan Huber of UIUC for taking high-resolution photographs of the poster; and we thank Laura Thurlwell of the Department of Plant Biology, also of UIUC, for typing this poster from the photograph of the poster. We are indebted to Mary Wraight for her permission to use Colin’s poster and to disseminate it for historical and educational purpose. Most importantly, we are highly thankful to Tony Crofts for editing the text produced by two of us (PM and Gov). PM thanks a grant that supports his research: TÁMOP 4.2.2.D-15/1/KONV-2015-0024.
- Ädelroth P, Paddock ML, Tehrani A, Beatty JT, Feher G, Okamura MY (2001) Identification of the proton pathway in bacterial reaction centers: decrease of proton transfer rate by mutation of surface histidines at H126 and H128 and chemical rescue by imidazole identifies the initial proton donors. Biochemistry 40:14538–14546PubMedCrossRefGoogle Scholar
- Berg JM, Tymoczko JL, Stryer L (2002) Chapter 18.4: a proton gradient powers the synthesis of ATP. In: Biochemistry, 5th edn. W. H. Freeman and Company, New YorkGoogle Scholar
- Govindjee, Prince RC, Ort DR (2015) Colin A. Wraight (1945–2014). Photosynth Res :20. doi:10.1007/s11120-015-0174-1
- Kis M, Asztalos E, Sipka G, Maróti P (2014) Assembly of photosynthetic apparatus in Rhodobacter sphaeroides as revealed by functional assessments at different growth phases and in synchronized and greening cells. Photosynth Res 122:261–273Google Scholar
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- Takahashi E, Wraight CA (1992) Proton and electron transfer in the acceptor quinone complex of Rhodobacter sphaeroides reaction centers: characterization of site-directed mutants of the two ionizable residues, GluL212 and AspL213, in the QB binding site. Biochemistry 31:855–866PubMedCrossRefGoogle Scholar
- Takahashi E, Wraight CA (1996) Potentiation of proton transfer function by electrostatic interactions in photosynthetic reaction centers from Rhodobacter sphaeroides: first results from site-directed mutation of the H subunit. Proc Natl Acad Sci USA 93:2640–2645PubMedPubMedCentralCrossRefGoogle Scholar
- Wraight CA (2005) Chapter 12: intraprotein proton transfer—concepts and realities from the bacterial photosynthetic reaction center. In: Wïkstrom M (ed) Biophysical and structural aspects of bioenergetics. RSC biomolecular science series. Royal Society of Chemistry, CambridgeGoogle Scholar