Theoretical studies on mechanisms of some Mo enzymes
Gespeichert in:
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)
Online Zugang:
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605507961 | ||
| 003 | CHVBK | ||
| 005 | 20210128100634.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20150301xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00775-015-1237-7 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00775-015-1237-7 | ||
| 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 |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 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 | ||