Structure and function of NADH : ubiquinone oxidoreductase (complex 1)

Project Information

Grant agreement ID: BIO2930364

Project closed

Start date 1 September 1993

End date 31 August 1996

Funded under

• Specific research and technological development programme (EEC) in the field of biotechnology, 1990-1994

Total cost No data

EU contribution € 836 000,00

Coordinated by

MRC Laboratory of Molecular Biology
United Kingdom

Objective

We have undertaken a joint study of the structural features of the mitochondrial, chloroplast and bacterial NADH-CoQ reductase (complex I) from bovine mitochondria, pea chloroplasts and from the bacterium Rhodobacter capsulatus.
Crystallization of a new crystal form of the sub-complex Ilambda fragment of bovine complex I. Sequence analysis of the 42nd subunit of bovine complex I. A 30 Å resolution structure of bovine complex I by single particle analysis electron microscopy. Location of the iron-sulphur clusters 2 in the TYKY subunit of bovine complex I. Demonstration that both a semiquinone radical and a 27structural change in the TYKY subunit of bovine complex I are involved in the coupling of electron transfer to proton translocation. Purification of a protein complex containing the chloroplast encoded protein Ndh K from the thylakoid membranes of chloroplasts from pea plants. Cloning and sequencing of the Rhodobacter nuo operon. Identification of transcriptional signals of Rhodobacter nuo operon. Site directed mutagenesis of Rhodobacter NUO1 (equivalent of bovine TYKY). Isolation of piericidin resistant mutants of Rhodobacter. Partial purification of Rhodobacter complex I.

MAJOR SCIENTIFIC BREAKTHROUGHS:
Structure of bovine complex I at 30 Å resolution. Production of a new 3D-crystal form of the sub-complex 1lambda fragment of bovine complex I. Sequence of a new subunit of bovine complex I. The TYKY subunit of bovine complex I contains Fe-S clusters that are linked via a semiubiquinone radical with the coupling of electron transfer to proton translocation. Purification of a protein complex containing Ndh K from pea chloroplasts. Sequence of the of the Rhodobacter nuo operon. Identification of transcriptional signals of the Rhodobacter nuo operon. Site directed mutants of Rhodobacter NUO1.

Fields of science

CORDIS classifies projects with EuroSciVoc, a multilingual taxonomy of fields of science, through a semi-automatic process based on NLP techniques.

• natural sciences › biological sciences › microbiology › bacteriology
• natural sciences › biological sciences › biochemistry › biomolecules › proteins
• natural sciences › physical sciences › optics › microscopy › electron microscopy

Programme(s)

• FP3-BIOTECH 1 - Specific research and technological development programme (EEC) in the field of biotechnology, 1990-1994

Topic(s)

• 1.1 - Protein structure and function

Call for proposal

Data not available

Funding Scheme

CSC - Cost-sharing contracts

Coordinator

MRC Laboratory of Molecular Biology

• EU contribution: No data
• Address: Hills Road ; CB2 2QH Cambridge ; United Kingdom
• Total cost: No data

Participants (3)

Commissariat à l'Energie Atomique (CEA)

France

• EU contribution: No data
• Address: Centre d'Etudes de Grenoble ; 38041 Grenoble
• Total cost: No data

Universidad del País Vasco

Spain

• EU contribution: No data
• Address: S/N,B Sarriena S/N ; 48940 Lejona
• Total cost: No data

Universiteit van Amsterdam

Netherlands

• EU contribution: No data
• Address: 127,Nieuwe Achtergracht 127 ; 1018 WS Amsterdam
• Total cost: No data