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Isotopic fractionation associated with [NiFe]- and [FeFe]-hydrogenases
Rapid communications in mass spectrometry, 2016-01, Vol.30 (2), p.285-292
Yang, Hui
Gandhi, Hasand
Cornish, Adam J.
Moran, James J.
Kreuzer, Helen W.
Ostrom, Nathaniel E.
Hegg, Eric L.
2016
Volltextzugriff (PDF)
Details
Autor(en) / Beteiligte
Yang, Hui
Gandhi, Hasand
Cornish, Adam J.
Moran, James J.
Kreuzer, Helen W.
Ostrom, Nathaniel E.
Hegg, Eric L.
Titel
Isotopic fractionation associated with [NiFe]- and [FeFe]-hydrogenases
Ist Teil von
Rapid communications in mass spectrometry, 2016-01, Vol.30 (2), p.285-292
Ort / Verlag
England: Blackwell Publishing Ltd
Erscheinungsjahr
2016
Quelle
Wiley Online Library - AutoHoldings Journals
Beschreibungen/Notizen
Rationale Hydrogenases catalyze the reversible formation of H2 from electrons and protons with high efficiency. Understanding the relationships between H2 production, H2 uptake, and H2‐H2O exchange can provide insight into the metabolism of microbial communities in which H2 is an essential component in energy cycling. Methods We used stable H isotopes (1H and 2H) to probe the isotope effects associated with three [FeFe]‐hydrogenases and three [NiFe]‐hydrogenases. Results All six hydrogenases displayed fractionation factors for H2 formation that were significantly less than 1, producing H2 that was severely depleted in 2H relative to the substrate, water. Consistent with differences in their active site structure, the fractionation factors for each class appear to cluster, with the three [NiFe]‐hydrogenases (α = 0.27–0.40) generally having smaller values than the three [FeFe]‐hydrogenases (α = 0.41–0.55). We also obtained isotopic fractionation factors associated with H2 uptake and H2‐H2O exchange under conditions similar to those utilized for H2 production, providing a more complete picture of the reactions catalyzed by hydrogenases. Conclusions The fractionation factors determined in our studies can be used as signatures for different hydrogenases to probe their activity under different growth conditions and to ascertain which hydrogenases are most responsible for H2 production and/or uptake in complex microbial communities. Copyright © 2015 John Wiley & Sons, Ltd.
Sprache
Englisch
Identifikatoren
ISSN: 0951-4198, 1097-0231
eISSN: 1097-0231
DOI: 10.1002/rcm.7432
Titel-ID: cdi_osti_scitechconnect_1236916
Format
–
Schlagworte
Chemical Fractionation
,
Chlamydomonas reinhardtii - enzymology
,
Clostridium - enzymology
,
Deuterium - chemistry
,
Hydrogen - chemistry
,
Hydrogenase - chemistry
,
Iron-Sulfur Proteins - chemistry
,
Shewanella - enzymology
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