caa a22 4500 605507961 CHVBK 20210128100634.0 cr unu---uuuuu 210128e20150301xx s 000 0 eng 10.1007/s00775-015-1237-7 doi (NATIONALLICENCE)springer-10.1007/s00775-015-1237-7 Theoretical studies on mechanisms of some Mo enzymes [Elektronische Daten] [Nuno Cerqueira, Bholanath Pakhira, Sabyasachi Sarkar] 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). SBIC, 2015 Oxomolybdoenzymes nationallicence Model reactions nationallicence Nitrate reductase nationallicence Formate dehydrogenase nationallicence Trimethylamine N-oxide reductase nationallicence Xanthine oxidase nationallicence Cerqueira Nuno REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal aut Pakhira Bholanath Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India aut Sarkar Sabyasachi Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India aut JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 323-335 0949-8257 20:2<323 2015 20 775 https://doi.org/10.1007/s00775-015-1237-7 text/html Onlinezugriff via DOI BK010053 XK010053 XK010000 Metadata rights reserved Springer special CC-BY-NC licence nationallicence 1 review-article jats NATIONALLICENCE NATIONALLICENCE NL-springer NATIONALLICENCE 856 40 https://doi.org/10.1007/s00775-015-1237-7 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Cerqueira Nuno REQUIMTE, Departamento de Química, Faculdade de Ciências, Universidade do Porto, Rua do Campo Alegre s/n, 4169-007, Porto, Portugal aut NATIONALLICENCE 700 1- Pakhira Bholanath Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India aut NATIONALLICENCE 700 1- Sarkar Sabyasachi Department of Chemistry, Indian Institute of Engineering Science and Technology, Shibpur, Botanic Garden, 711103, Howrah, West Bengal, India aut NATIONALLICENCE 773 0- JBIC Journal of Biological Inorganic Chemistry Springer Berlin Heidelberg 20/2(2015-03-01), 323-335 0949-8257 20:2<323 2015 20 775