A hybrid of the transhydrogenases from Rhodospirillum rubrum and mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-trans locating reaction

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@article{64b5c855bd5d4b36bd456966f221fd2f,
title = "A hybrid of the transhydrogenases from Rhodospirillum rubrum and mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-trans locating reaction",
abstract = "All transhydrogenases appear to have three components: dI, which binds NAD(H), and dIII, which binds NADP(H), protrude from the membrane, and dII spans the membrane. However, the polypeptide composition of the enzymes varies amongst species. The transhydrogenases of Mycobacterium tuberculosis and of Rhodospirillum rubrum have three polypeptides. Sequence analysis indicates that an ancestral three-polypeptide enzyme evolved into transhydrogenases with either two polypeptides (such as the Escherichia coli enzyme) or one polypeptide (such as the mitochondrial enzyme). The fusion steps in each case probably led to the development of an additional transmembrane helix. A hybrid transhydrogenase was constructed from the dI component of the M. tuberculosis enzyme and the dII and dIII components of the R. rubrum enzyme. The hybrid catalyses cyclic transhydrogenation but not the proton-translocating, reverse reaction. This shows that nucleotide-binding/release at the NAD(H) site, and hydride transfer, are fully functional but that events associated with NADP(H) binding/release are compromised. It is concluded that sequence mismatch in the hybrid prevents a conformational change between dI and dIII which is essential for the step accompanying proton translocation. (c) 2006 Elsevier B.V. All rights reserved.",
keywords = "nicotinamide nucleotides, proton translocation, phylogenetic tree, Rhodospirillum rubrum, transhydrogenase, Mycobacterium tuberculosis",
author = "R Wilson and U Obiozo and PG Quirk and Gurdyal Besra and John Jackson",
year = "2006",
month = mar,
day = "1",
doi = "10.1016/j.bbabio.2006.03.004",
language = "English",
volume = "1757",
pages = "215--223",
journal = "Biochimica et Biophysica Acta",
issn = "1874-9399",
publisher = "Elsevier",
number = "3",

}

RIS

TY - JOUR

T1 - A hybrid of the transhydrogenases from Rhodospirillum rubrum and mycobacterium tuberculosis catalyses rapid hydride transfer but not the complete, proton-trans locating reaction

AU - Wilson, R

AU - Obiozo, U

AU - Quirk, PG

AU - Besra, Gurdyal

AU - Jackson, John

PY - 2006/3/1

Y1 - 2006/3/1

N2 - All transhydrogenases appear to have three components: dI, which binds NAD(H), and dIII, which binds NADP(H), protrude from the membrane, and dII spans the membrane. However, the polypeptide composition of the enzymes varies amongst species. The transhydrogenases of Mycobacterium tuberculosis and of Rhodospirillum rubrum have three polypeptides. Sequence analysis indicates that an ancestral three-polypeptide enzyme evolved into transhydrogenases with either two polypeptides (such as the Escherichia coli enzyme) or one polypeptide (such as the mitochondrial enzyme). The fusion steps in each case probably led to the development of an additional transmembrane helix. A hybrid transhydrogenase was constructed from the dI component of the M. tuberculosis enzyme and the dII and dIII components of the R. rubrum enzyme. The hybrid catalyses cyclic transhydrogenation but not the proton-translocating, reverse reaction. This shows that nucleotide-binding/release at the NAD(H) site, and hydride transfer, are fully functional but that events associated with NADP(H) binding/release are compromised. It is concluded that sequence mismatch in the hybrid prevents a conformational change between dI and dIII which is essential for the step accompanying proton translocation. (c) 2006 Elsevier B.V. All rights reserved.

AB - All transhydrogenases appear to have three components: dI, which binds NAD(H), and dIII, which binds NADP(H), protrude from the membrane, and dII spans the membrane. However, the polypeptide composition of the enzymes varies amongst species. The transhydrogenases of Mycobacterium tuberculosis and of Rhodospirillum rubrum have three polypeptides. Sequence analysis indicates that an ancestral three-polypeptide enzyme evolved into transhydrogenases with either two polypeptides (such as the Escherichia coli enzyme) or one polypeptide (such as the mitochondrial enzyme). The fusion steps in each case probably led to the development of an additional transmembrane helix. A hybrid transhydrogenase was constructed from the dI component of the M. tuberculosis enzyme and the dII and dIII components of the R. rubrum enzyme. The hybrid catalyses cyclic transhydrogenation but not the proton-translocating, reverse reaction. This shows that nucleotide-binding/release at the NAD(H) site, and hydride transfer, are fully functional but that events associated with NADP(H) binding/release are compromised. It is concluded that sequence mismatch in the hybrid prevents a conformational change between dI and dIII which is essential for the step accompanying proton translocation. (c) 2006 Elsevier B.V. All rights reserved.

KW - nicotinamide nucleotides

KW - proton translocation

KW - phylogenetic tree

KW - Rhodospirillum rubrum

KW - transhydrogenase

KW - Mycobacterium tuberculosis

UR - http://www.scopus.com/inward/record.url?scp=33646111905&partnerID=8YFLogxK

U2 - 10.1016/j.bbabio.2006.03.004

DO - 10.1016/j.bbabio.2006.03.004

M3 - Article

C2 - 16624251

VL - 1757

SP - 215

EP - 223

JO - Biochimica et Biophysica Acta

JF - Biochimica et Biophysica Acta

SN - 1874-9399

IS - 3

ER -