Complex I from the fungus Neurospora crassa

Biochim Biophys Acta. 1998 May 6;1364(2):89-100. doi: 10.1016/s0005-2728(98)00020-6.

Abstract

Respiratory chain complex I is a complicated enzyme of mitochondria, that couples electron transfer from NADH to ubiquinone to the proton translocation across the inner membrane of the organelle. The fungus Neurospora crassa has been used as one of the main model organisms to study this enzyme. Complex I is composed of multiple polypeptide subunits of dual genetic origin and contains several prosthetic groups involved in its activity. Most subunits have been cloned and those binding redox centres have been identified. Yet, the functional role of certain complex I proteins remains unknown. Insight into the possible origin and the mechanisms of complex I assembly has been gained. Several mutant strains of N. crassa, in which specific subunits of complex I were disrupted, have been isolated and characterised. This review concerns many aspects of the structure, function and biogenesis of complex I that are being elucidated.

Publication types

  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amino Acid Sequence
  • Animals
  • Cattle
  • Molecular Sequence Data
  • NAD(P)H Dehydrogenase (Quinone)* / chemistry
  • NAD(P)H Dehydrogenase (Quinone)* / genetics
  • NAD(P)H Dehydrogenase (Quinone)* / metabolism
  • Neurospora crassa / enzymology*

Substances

  • NAD(P)H Dehydrogenase (Quinone)