Literature DB >> 10682839

Unusual FTIR and EPR properties of the H2-activating site of the cytoplasmic NAD-reducing hydrogenase from Ralstonia eutropha.

R P Happe1, W Roseboom, G Egert, C G Friedrich, C Massanz, B Friedrich, S P Albracht.   

Abstract

Soluble NAD-reducing [NiFe]-hydrogenase (SH) from Ralstonia eutropha (formerly Alcaligenes eutrophus) has an infrared spectrum with one strong band at 1956 cm(-1) and four weak bands at 2098, 2088, 2081 and 2071 cm(-1) in the 2150-1850 cm(-1) spectral region. Other [NiFe]-hydrogenases only show one strong and two weak bands in this region, attributable to the NiFe(CN)2(CO) active site. The position of these three bands is highly sensitive to redox changes of the active site. In contrast, reduction of the SH resulted in a shift to lower frequencies of the 2098 cm(-1) band only. These and other properties prompted us to propose the presence of a Ni(CN)Fe(CN)3(CO) active site.

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Year:  2000        PMID： 10682839     DOI： 10.1016/s0014-5793(99)01799-8

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  11 in total

1.  An improved purification procedure for the soluble [NiFe]-hydrogenase of Ralstonia eutropha: new insights into its (in)stability and spectroscopic properties.

Authors:  Eddy van der Linden; Tanja Burgdorf; Antonio L de Lacey; Thorsten Buhrke; Marcel Scholte; Victor M Fernandez; Bärbel Friedrich; Simon P J Albracht
Journal:  J Biol Inorg Chem       Date:  2006-01-18       Impact factor: 3.358

2.  The soluble NAD+-Reducing [NiFe]-hydrogenase from Ralstonia eutropha H16 consists of six subunits and can be specifically activated by NADPH.

Authors:  Tanja Burgdorf; Eddy van der Linden; Michael Bernhard; Qing Yuan Yin; Jaap W Back; Aloysius F Hartog; Anton O Muijsers; Chris G de Koster; Simon P J Albracht; Bärbel Friedrich
Journal:  J Bacteriol       Date:  2005-05       Impact factor: 3.490

3.  Sustained photoevolution of molecular hydrogen in a mutant of Synechocystis sp. strain PCC 6803 deficient in the type I NADPH-dehydrogenase complex.

Authors:  Laurent Cournac; Geneviève Guedeney; Gilles Peltier; Paulette M Vignais
Journal:  J Bacteriol       Date:  2004-03       Impact factor: 3.490

4.  Functional analysis by site-directed mutagenesis of the NAD(+)-reducing hydrogenase from Ralstonia eutropha.

Authors:  Tanja Burgdorf; Antonio L De Lacey; Bärbel Friedrich
Journal:  J Bacteriol       Date:  2002-11       Impact factor: 3.490

5.  Enzymatic and spectroscopic properties of a thermostable [NiFe]‑hydrogenase performing H2-driven NAD+-reduction in the presence of O2.

Authors:  Janina Preissler; Stefan Wahlefeld; Christian Lorent; Christian Teutloff; Marius Horch; Lars Lauterbach; Stephen P Cramer; Ingo Zebger; Oliver Lenz
Journal:  Biochim Biophys Acta Bioenerg       Date:  2017-09-29       Impact factor: 3.991

6.  Overexpression, isolation, and spectroscopic characterization of the bidirectional [NiFe] hydrogenase from Synechocystis sp. PCC 6803.

Authors:  Frauke Germer; Ingo Zebger; Miguel Saggu; Friedhelm Lendzian; Rüdiger Schulz; Jens Appel
Journal:  J Biol Chem       Date:  2009-09-28       Impact factor: 5.157

7.  Spectroscopic insights into the oxygen-tolerant membrane-associated [NiFe] hydrogenase of Ralstonia eutropha H16.

Authors:  Miguel Saggu; Ingo Zebger; Marcus Ludwig; Oliver Lenz; Bärbel Friedrich; Peter Hildebrandt; Friedhelm Lendzian
Journal:  J Biol Chem       Date:  2009-03-20       Impact factor: 5.157

8.  The soluble [NiFe]-hydrogenase from Ralstonia eutropha contains four cyanides in its active site, one of which is responsible for the insensitivity towards oxygen.

Authors:  Eddy Van der Linden; Tanja Burgdorf; Michael Bernhard; Boris Bleijlevens; Bärbel Friedrich; Simon P J Albracht
Journal:  J Biol Inorg Chem       Date:  2004-05-26       Impact factor: 3.358

9.  Catalytic properties of the isolated diaphorase fragment of the NAD-reducing [NiFe]-hydrogenase from Ralstonia eutropha.

Authors:  Lars Lauterbach; Zulkifli Idris; Kylie A Vincent; Oliver Lenz
Journal:  PLoS One       Date:  2011-10-10       Impact factor: 3.240

10.  An innovative cloning platform enables large-scale production and maturation of an oxygen-tolerant [NiFe]-hydrogenase from Cupriavidus necator in Escherichia coli.

Authors:  Johannes Schiffels; Olaf Pinkenburg; Maximilian Schelden; El-Hussiny A A Aboulnaga; Marcus E M Baumann; Thorsten Selmer
Journal:  PLoS One       Date:  2013-07-05       Impact factor: 3.240
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