Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum .DELTA.H

Alex, Lisa A.; Reeve, John N.; Orme‐Johnson, William H.; Walsh, Christopher T.

doi:10.1021/bi00483a011

Cited by 93 publications

(25 citation statements)

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“…These enzymes consist of a large subunit (FrhA), a small subunit (FrhG), and a FAD containing-subunit (FrhB) for electron transfer to F 420 [82,83].…”

Section: Group 2bmentioning

confidence: 99%

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Peters

Schut

Boyd

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

410

397

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The [FeFe]- and [NiFe]-hydrogenases catalyze the formal interconversion between hydrogen and protons and electrons, possess characteristic non-protein ligands at their catalytic sites and thus share common mechanistic features. Despite the similarities between these two types of hydrogenases, they clearly have distinct evolutionary origins and likely emerged from different selective pressures. [FeFe]-hydrogenases are widely distributed in fermentative anaerobic microorganisms and likely evolved under selective pressure to couple hydrogen production to the recycling of electron carriers that accumulate during anaerobic metabolism. In contrast, many [NiFe]-hydrogenases catalyze hydrogen oxidation as part of energy metabolism and were likely key enzymes in early life and arguably represent the predecessors of modern respiratory metabolism. Although the reversible combination of protons and electrons to generate hydrogen gas is the simplest of chemical reactions, the [FeFe]- and [NiFe]-hydrogenases have distinct mechanisms and differ in the fundamental chemistry associated with proton transfer and control of electron flow that also help to define catalytic bias. A unifying feature of these enzymes is that hydrogen activation itself has been restricted to one solution involving diatomic ligands (carbon monoxide and cyanide) bound to an Fe ion. On the other hand, and quite remarkably, the biosynthetic mechanisms to produce these ligands are exclusive to each type of enzyme. Furthermore, these mechanisms represent two independent solutions to the formation of complex bioinorganic active sites for catalyzing the simplest of chemical reactions, reversible hydrogen oxidation. As such, the [FeFe]- and [NiFe]-hydrogenases are arguably the most profound case of convergent evolution. This article is part of a Special Issue entitled: Fe/S proteins: Analysis, structure, function, biogenesis and diseases.

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“…These enzymes consist of a large subunit (FrhA), a small subunit (FrhG), and a FAD containing-subunit (FrhB) for electron transfer to F 420 [82,83].…”

Section: Group 2bmentioning

confidence: 99%

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Peters

Schut

Boyd

et al. 2015

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research

410

397

View full text Add to dashboard Cite

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“…Red arrows represent electron transfer, while dashed blue arrows show chemiosmotic ion movement. Enzyme abbreviations and references for the enzymes indicated are: Frh, F 420 -reducing hydrogenase (2); Ech, energy-conserving hydrogenase (101, 112); Vho, methanophenazine-reducing hydrogenase (22); Fpo/Fqo, F 420 H 2 : phenazine/quinone oxidoreductase (7); HdrDE, heterodisulfide reductase (21); Mhc, Multiheme cytochrome (57); Rnf, Na + -translocating, ferredoxin:NAD oxidoreductase (88); Mtr, Na + -translocating methyl-H 4 MPT:coenzyme M methyltransferase (9, 45). …”

Section: Figmentioning

confidence: 99%

Energy Metabolism during Anaerobic Methane Oxidation in ANME Archaea

McGlynn

2017

Microbes and environments

107

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Anaerobic methane oxidation in archaea is often presented to operate via a pathway of “reverse methanogenesis”. However, if the cumulative reactions of a methanogen are run in reverse there is no apparent way to conserve energy. Recent findings suggest that chemiosmotic coupling enzymes known from their use in methylotrophic and acetoclastic methanogens—in addition to unique terminal reductases—biochemically facilitate energy conservation during complete CH4 oxidation to CO2. The apparent enzyme modularity of these organisms highlights how microbes can arrange their energy metabolisms to accommodate diverse chemical potentials in various ecological niches, even in the extreme case of utilizing “reverse” thermodynamic potentials.

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“…The genes for the F420-reducing hydrogenase, frhADGB, and the non-F420-reducing hydrogenase, mvhDGAB (2,37) The present communication reports on a systematic electron microscopic investigation of the F420-reducing hydrogenase and the non-F420-reducing hydrogenase isolated from M. thermoautotrophicum Marburg. It combines data obtained by conventional transmission electron microscopy of negatively stained samples, tilting experiments, application of electron spectroscopic imaging (ESI) (5,38), and immunogold labelling experiments.…”

mentioning

confidence: 92%

“…Two types of hydrogenase have been detected in numerous methanogenic bacteria, including M. thermoautotrophicum (3,7,9,10,13,21,25,27,29,36,37,48), i.e., an F420 (8-hydroxy-5-deazaflavin)-reducing hydrogenase and a non-F420-reducing hydrogenase, both of which can be assayed via the reduction of viologen dyes with H2 (16). The F420-reducing hydrogenase also reduces the physiological two-electron acceptor F420.The F420-reducing hydrogenase contains approximately 0.7 mol of nickel, 0.9 mol of flavinadenine dinucleotide, and 13 to 14 mol of nonheme iron and acid-labile sulfur per mol of alp1,yj (2,12). The non-F420-reducing hydrogenase contains nickel and iron-sulfur clusters in undetermined amounts (18).…”

mentioning

confidence: 99%

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Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg

et al. 1994

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The F420-reducing hydrogenase and the non-F420-reducing hydrogenase (EC 1.12.99.1.) were isolated from a crude extract of Methanobacterium thermoautotrophicum Marburg. Electron microscopy of the negatively stained F420-reducing hydrogenase revealed that the enzyme is a complex with a diameter of 15.6 nm. It consists of two ring-like, stacked, parallel layers each composed of three major protein masses arranged in rotational symmetry. Each of these masses appeared to be subdivided into smaller protein masses. Electron microscopy of negatively stained samples taken from intermediate steps of the purification process revealed the presence of enzyme particles bound to inside-out membrane vesicles. Linker particles of 10 to 20 kDa which mediate the attachment of the hydrogenase to the cytoplasmic membrane were seen. Immunogold labelling confirmed that the F420-reducing hydrogenase is a membrane-bound enzyme. Electron microscopy of the negatively stained purified non-F420-reducing hydrogenase revealed that the enzyme is composed of three subunits exhibiting different diameters (5, 4, and 2 to 3 nm). According to immunogold labelling experiments, approximately 70% of the non-F420-reducing hydrogenase protein molecules were located at the cell periphery; the remaining 30% were cytoplasmic. No linker particles were observed for this enzyme.The methanogenic archaebacterium Methanobacterium thermoautotrophicum Marburg (DSM 2133) grows on H2 and CO2 as sole electron, carbon, and energy sources (14). Two types of hydrogenase have been detected in numerous methanogenic bacteria, including M. thermoautotrophicum (3,7,9,10,13,21,25,27,29,36,37,48), i.e., an F420 (8-hydroxy-5-deazaflavin)-reducing hydrogenase and a non-F420-reducing hydrogenase, both of which can be assayed via the reduction of viologen dyes with H2 (16). The F420-reducing hydrogenase also reduces the physiological two-electron acceptor F420.The F420-reducing hydrogenase contains approximately 0.7 mol of nickel, 0.9 mol of flavinadenine dinucleotide, and 13 to 14 mol of nonheme iron and acid-labile sulfur per mol of alp1,yj (2,12). The non-F420-reducing hydrogenase contains nickel and iron-sulfur clusters in undetermined amounts (18).The non-F420-reducing hydrogenase is part of an H2-heterodisulfide oxidoreductase complex in the methylotrophic bacterium Methanosarcina barkeri (19) and the hydrogenotrophic bacterium M. thermoautotrophicum. In the methylotrophic organism, this complex also contains cytochrome b and is tightly membrane associated (19), whereas the complex in the hydrogenotrophic organism contains no cytochromes and is weakly membrane associated (41). In the methylotrophic organism, electrons are transferred via these cytochromes to the heterodisulfide reductase, thereby generating a proton potential (7, 8), whereas the electron carrier in the hydrogenotrophic organism remains unknown. The present communication reports on a systematic electron microscopic investigation of the F420-reducing hydrogenase and the non-F420-reducing hydrogenase isolated f...

show abstract

Cloning, sequence determination, and expression of the genes encoding the subunits of the nickel-containing 8-hydroxy-5-deazaflavin reducing hydrogenase from Methanobacterium thermoautotrophicum .DELTA.H

Cited by 93 publications

References 48 publications

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

[FeFe]- and [NiFe]-hydrogenase diversity, mechanism, and maturation

Energy Metabolism during Anaerobic Methane Oxidation in ANME Archaea

Structural aspects and immunolocalization of the F420-reducing and non-F420-reducing hydrogenases from Methanobacterium thermoautotrophicum Marburg

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