JBIC Journal of Biological Inorganic Chemistry

, Volume 13, Issue 8, pp 1185–1195

Enzymatic activity mastered by altering metal coordination spheres

  • Isabel Moura
  • Sofia R. Pauleta
  • José J. G. Moura
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DOI: 10.1007/s00775-008-0414-3

Cite this article as:
Moura, I., Pauleta, S.R. & Moura, J.J.G. J Biol Inorg Chem (2008) 13: 1185. doi:10.1007/s00775-008-0414-3

Abstract

Metalloenzymes control enzymatic activity by changing the characteristics of the metal centers where catalysis takes place. The conversion between inactive and active states can be tuned by altering the coordination number of the metal site, and in some cases by an associated conformational change. These processes will be illustrated using heme proteins (cytochrome c nitrite reductase, cytochrome c peroxidase and cytochrome cd1 nitrite reductase), non-heme proteins (superoxide reductase and [NiFe]-hydrogenase), and copper proteins (nitrite and nitrous oxide reductases) as examples. These examples catalyze electron transfer reactions that include atom transfer, abstraction and insertion.

Keywords

Enzyme activationActive site coordinationHemeCopper and non-heme proteins

Abbreviations

ccNIR

Cytochrome c nitrite reductase

CuNIR

Copper nitrite reductase

Copyright information

© SBIC 2008

Authors and Affiliations

  • Isabel Moura
    • 1
  • Sofia R. Pauleta
    • 1
  • José J. G. Moura
    • 1
  1. 1.REQUIMTE, Centro de Química Fina e Biotecnologia, Departamento de Química, Faculdade de Ciências e TecnologiaUniversidade Nova de LisboaCaparicaPortugal