Theoretical studies on mechanisms of some Mo enzymes

Verfasser / Beitragende:
[Nuno Cerqueira, Bholanath Pakhira, Sabyasachi Sarkar]
Ort, Verlag, Jahr:
2015
Enthalten in:
JBIC Journal of Biological Inorganic Chemistry, 20/2(2015-03-01), 323-335
Format:
Artikel (online)
ID: 605507961
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024 7 0 |a 10.1007/s00775-015-1237-7  |2 doi 
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245 0 0 |a Theoretical studies on mechanisms of some Mo enzymes  |h [Elektronische Daten]  |c [Nuno Cerqueira, Bholanath Pakhira, Sabyasachi Sarkar] 
520 3 |a Modeling of molybdoenzymes began even before the knowledge of the three-dimensional structure of these enzymes. The theoretical and experimental knowledge on these enzymes is vast and newer investigation is regularly pursued to understand the electronic aspect of these proteins using computational means. The present review deals with some unique observation regarding the structure, function and reactivity of some models and native proteins in rationalizing the choice of diverse substrates in seemingly similar enzymes such as Nap (nitrate reductase) and Fdh (formate dehydrogenase) and the dual form of a specific substrate of an enzyme like trimethylamine N-oxide reductase (TAMOR) and providing the electronic reason for the inhibition in the oxypurinol-inhibited xanthine oxidase (XO). 
540 |a SBIC, 2015 
690 7 |a Oxomolybdoenzymes  |2 nationallicence 
690 7 |a Model reactions  |2 nationallicence 
690 7 |a Nitrate reductase  |2 nationallicence 
690 7 |a Formate dehydrogenase  |2 nationallicence 
690 7 |a Trimethylamine N-oxide reductase  |2 nationallicence 
690 7 |a Xanthine oxidase  |2 nationallicence 
700 1 |a Cerqueira  |D Nuno  |u REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal  |4 aut 
700 1 |a Pakhira  |D Bholanath  |u Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India  |4 aut 
700 1 |a Sarkar  |D Sabyasachi  |u Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India  |4 aut 
773 0 |t JBIC Journal of Biological Inorganic Chemistry  |d Springer Berlin Heidelberg  |g 20/2(2015-03-01), 323-335  |x 0949-8257  |q 20:2<323  |1 2015  |2 20  |o 775 
856 4 0 |u https://doi.org/10.1007/s00775-015-1237-7  |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/s00775-015-1237-7  |q text/html  |z Onlinezugriff via DOI 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Cerqueira  |D Nuno  |u REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Pakhira  |D Bholanath  |u Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India  |4 aut 
950 |B NATIONALLICENCE  |P 700  |E 1-  |a Sarkar  |D Sabyasachi  |u Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India  |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), 323-335  |x 0949-8257  |q 20:2<323  |1 2015  |2 20  |o 775