From NADH to ubiquinone in Neurospora mitochondria

• Type: Article in International Scientific Journal
• Date: 2002

Authors

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

Journal

Title: Biochimica et Biophysica Acta - Bioenergetics

Vol. 1555

Pages: 187-191

ISSN: 0005-2728

Publisher: Elsevier

Indexing

ISI Web of Knowledge - 65 Citations

Scopus - 64 Citations

Other information

Authenticus ID: 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.

Language: English

Type (Professor's evaluation): Scientific

No. of pages: 5