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J. Biol. Chem., Vol. 275, Issue 24, 17968-17973, June 16, 2000
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From the The F420H2 dehydrogenase
is part of the energy conserving electron transport system of the
methanogenic archaeon Methanosarcina mazei Gö1. Here
it is shown that cofactor
F420H2-dependent reduction of
2-hydroxyphenazine as catalyzed by the membrane-bound enzyme is coupled
to proton translocation across the cytoplasmic membrane, exhibiting a
stoichiometry of 0.9 H+ translocated per two electrons
transferred. The electrochemical proton gradient thereby generated was
shown to drive ATP synthesis from ADP + Pi. The gene
cluster encoding the F420H2 dehydrogenase of
M. mazei Gö1 comprises 12 genes that are referred to
as fpoA, B, C, D,
H, I, J, K,
L, M, N, and O.
Analysis of the deduced amino acid sequences revealed that the enzyme
is closely related to proton translocating NADH dehydrogenases of
respiratory chains from bacteria (NDH-1) and eukarya (complex I). Like
the NADH-dependent enzymes, the
F420H2 dehydrogenase is composed of three
subcomplexes. The gene products FpoA, H, J, K, L, M, and N are highly
hydrophobic and are homologous to subunits that form the membrane
integral module of NDH-1. FpoB, C, D, and I have their counterparts in the amphipathic membrane-associated module of NDH-1. Homologues to the
hydrophilic NADH-oxidizing input module are not present in M. mazei Gö1. Instead, the gene product FpoF may be
responsible for F420H2 oxidation and may
function as the electron input part. Thus, the
F420H2 dehydrogenase from M. mazei
Gö1 resembles eukaryotic and bacterial proton translocating NADH
dehydrogenases in many ways. The enzyme from the methanogenic archaeon
functions as a NDH-1/complex I homologue and is equipped with an
alternative electron input unit for the oxidation of reduced cofactor
F420 and a modified output module adopted to the reduction
of methanophenazine.
The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF228525 and AF228526.
The F420H2 Dehydrogenase from
Methanosarcina mazei Is a Redox-driven Proton Pump
Closely Related to NADH Dehydrogenases*
,,§, and¶
Abteilung Allgemeine Mikrobiologie and
§ Göttingen Genomics Laboratory, Institut für
Mikrobiologie und Genetik, Georg-August-Universität,
Grisebachstrasse 8, 37077 Göttingen, Germany
*
This work was supported by Grant De 488/4-2 of the Deutsche
Forschungsgemeinschaft (Bonn-Bad Godesberg), by the Deutsche
Forschungsgemeinschaft priority program "Structure of functional
modules from energy-transducing complexes in prokaryotes" Grant De
488/6-1, and by a grant from the Ministry of Science and Culture of the
state Lower Saxony.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
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