Open AccessDivision of labor in transhydrogenase by alternating proton translocation and hydride transfer
Author(s) -
Josephine H. Leung,
Lici A. Schurig-Briccio,
Mutsuo Yamaguchi,
Arne Moeller,
Jeffrey A. Speir,
Robert B. Gennis,
C.D. Stout
Publication year - 2015
Publication title -
science
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 12.556
H-Index - 1186
eISSN - 1095-9203
pISSN - 0036-8075
DOI - 10.1126/science.1260451
Subject(s) - thermus thermophilus , membrane , chemistry , enzyme , nad+ kinase , hydride , dimer , oxidoreductase , domain (mathematical analysis) , biochemistry , stereochemistry , biophysics , biology , escherichia coli , hydrogen , gene , mathematics , organic chemistry , mathematical analysis
Dueling dimers serve dual purposes Both bacteria and mitochrondria produce NADPH for amino acid biosynthesis and to remove reactive oxygen species. The enzyme that makes NADPH must translocate a proton across the membrane and transfer a hydride from NADH to NADP+ —processes that happen some 40 Å apart. To understand this complex geometry, Leunget al. solved the structures of the entire transhydrogenase enzyme and the membrane domain from the bacteriumThermus thermophilus (see the Perspective by Krengel and Törnroth-Horsefield). The entire enzyme exists as a dimer, with the two membrane domains in alternate orientations. One of the membrane domains interacts with the membrane component for proton translocation, whereas the other domain exchanges hydride with NAD(H) in another large soluble domain.Science , this issue p.178 ; see also p.125
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