Nitrogenase and homologs

Verfasser / Beitragende:
[Yilin Hu, Markus Ribbe]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/2(2015-03-01), 435-445
Format:
Artikel (online)
ID: 605507945
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024 7 0 |a 10.1007/s00775-014-1225-3  |2 doi 
035 |a (NATIONALLICENCE)springer-10.1007/s00775-014-1225-3 
245 0 0 |a Nitrogenase and homologs  |h [Elektronische Daten]  |c [Yilin Hu, Markus Ribbe] 
520 3 |a Nitrogenase catalyzes biological nitrogen fixation, a key step in the global nitrogen cycle. Three homologous nitrogenases have been identified to date, along with several structural and/or functional homologs of this enzyme that are involved in nitrogenase assembly, bacteriochlorophyll biosynthesis and methanogenic process, respectively. In this article, we provide an overview of the structures and functions of nitrogenase and its homologs, which highlights the similarity and disparity of this uniquely versatile group of enzymes. 
540 |a SBIC, 2014 
690 7 |a Nitrogenase  |2 nationallicence 
690 7 |a N2/CO/CO2 reduction  |2 nationallicence 
690 7 |a Radical SAM  |2 nationallicence 
690 7 |a Interstitial carbide  |2 nationallicence 
690 7 |a Homolog  |2 nationallicence 
690 7 |a EPR : Electron paramagnetic resonance  |2 nationallicence 
690 7 |a ENDOR : Electron-nuclear double resonance  |2 nationallicence 
690 7 |a ESEEM : Electron spin echo envelope modulation  |2 nationallicence 
690 7 |a EXAFS : Extended X-ray absorption fine structure  |2 nationallicence 
690 7 |a Fe protein : Iron protein  |2 nationallicence 
690 7 |a FeFe protein : Iron-iron protein  |2 nationallicence 
690 7 |a MoFe protein : Molybdenum-iron protein  |2 nationallicence 
690 7 |a SAXS : Small angle X-ray scattering  |2 nationallicence 
690 7 |a VFe protein : Vanadium-iron protein  |2 nationallicence 
690 7 |a XAS : X-ray absorption spectroscopy  |2 nationallicence 
690 7 |a XES : X-ray emission spectroscopy  |2 nationallicence 
700 1 |a Hu  |D Yilin  |u Department of Molecular Biology and Biochemistry, 2230 McGaugh Hall, University of California, 92697-3900, Irvine, CA, USA  |4 aut 
700 1 |a Ribbe  |D Markus  |u Department of Molecular Biology and Biochemistry, 2236 McGaugh Hall, University of California, 92697-3900, Irvine, CA, USA  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/2(2015-03-01), 435-445  |x 0949-8257  |q 20:2<435  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-014-1225-3  |q text/html  |z Onlinezugriff via DOI 
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900 7 |a Metadata rights reserved  |b Springer special CC-BY-NC licence  |2 nationallicence 
908 |D 1  |a review-article  |2 jats 
949 |B NATIONALLICENCE  |F NATIONALLICENCE  |b NL-springer 
950 |B NATIONALLICENCE  |P 856  |E 40  |u https://doi.org/10.1007/s00775-014-1225-3  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Hu  |D Yilin  |u Department of Molecular Biology and Biochemistry, 2230 McGaugh Hall, University of California, 92697-3900, Irvine, CA, USA  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Ribbe  |D Markus  |u Department of Molecular Biology and Biochemistry, 2236 McGaugh Hall, University of California, 92697-3900, Irvine, CA, USA  |4 aut 
950 |B NATIONALLICENCE  |P 773  |E 0-  |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/2(2015-03-01), 435-445  |x 0949-8257  |q 20:2<435  |1 2015  |2 20  |o 775