From NADH to ubiquinone in Neurospora mitochondria

• Tipo: Artigo em Revista Científica Internacional
• Data: 2002

Autores

videira, a (Autor) ICBAS; duarte, m (Autor) ICBAS

Revista

Título: Biochimica et Biophysica Acta - Bioenergetics

Vol. 1555

Páginas: 187-191

ISSN: 0005-2728

Editora: Elsevier

Indexação

ISI Web of Knowledge - 65 Citações

Scopus - 64 Citações

Outras Informações

ID Authenticus: P-000-MZY

DOI: 10.1016/S0005-2728(02)00276-1

Abstract (EN): The respiratory chain of the mitochondrial inner membrane includes a proton-pumping enzyme, complex I, which catalyses electron transfer from NADH to ubiquinone. This electron pathway occurs through a series of protein-bound prosthetic groups, FMN and around eight iron-sulfur clusters. The high number of polypeptide subunits of mitochondrial complex I, around 40, have a dual genetic origin. Neurospora crassa has been a useful genetic model to characterise complex I. The characterisation of mutants in specific proteins helped to understand the elaborate processes of the biogenesis, structure and function of the oligomeric enzyme. In the fungus, complex I seems to be dispensable for vegetative growth but required for sexual development. N. crassa mitochondria also contain three to four nonproton-pumping alternative NAD(P)H dehydrogenases. One of them is located in the outer face of the inner mitochondrial membrane, working as a calcium-dependent oxidase of cytosolic NADPH. (C) 2002 Elsevier Science B.V. All rights reserved.

Idioma: Inglês

Tipo (Avaliação Docente): Científica

Nº de páginas: 5