A Structural Perspective on Respiratory Complex I: Structure and Function of NADH:ubiquinone oxidoreductase
Editat de Leonid Sazanoven Limba Engleză Paperback – 11 iun 2014
Toate formatele și edițiile | Preț | Express |
---|---|---|
Paperback (1) | 1063.04 lei 6-8 săpt. | |
SPRINGER NETHERLANDS – 11 iun 2014 | 1063.04 lei 6-8 săpt. | |
Hardback (1) | 1070.46 lei 6-8 săpt. | |
SPRINGER NETHERLANDS – 16 mai 2012 | 1070.46 lei 6-8 săpt. |
Preț: 1063.04 lei
Preț vechi: 1118.99 lei
-5% Nou
Puncte Express: 1595
Preț estimativ în valută:
203.44€ • 213.97$ • 169.46£
203.44€ • 213.97$ • 169.46£
Carte tipărită la comandă
Livrare economică 03-17 ianuarie 25
Preluare comenzi: 021 569.72.76
Specificații
ISBN-13: 9789401783347
ISBN-10: 9401783349
Pagini: 296
Ilustrații: X, 286 p.
Dimensiuni: 155 x 235 x 16 mm
Greutate: 0.42 kg
Ediția:2012
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
ISBN-10: 9401783349
Pagini: 296
Ilustrații: X, 286 p.
Dimensiuni: 155 x 235 x 16 mm
Greutate: 0.42 kg
Ediția:2012
Editura: SPRINGER NETHERLANDS
Colecția Springer
Locul publicării:Dordrecht, Netherlands
Public țintă
ResearchCuprins
Part I: Structure and mechanism of complex I. - 1. Structure of complex I. - 2. On the mechanism of the respiratory complex I. - 3. Iron–sulfur clusters in complex I. - 4. Current Topics of the Inhibitors of Mitochondrial Complex I. - 5. My Fifty Years Association with Complex I Study. - Part II: Evolution of complex I. - 6. The Evolutionary Relationship between Complex I and [NiFe]-hydrogenase. - 7. Recruitment of the antiporter module - a key event in complex I evolution. - Part III: Mutations in complex I subunits and medical implications. - 8. Characterization of Bacterial Complex I (NDH-1) by a Genetic Engineering Approach. - 9. Cellular consequences of mtDNA-encoded mutations in NADH:ubiquinone oxidoreductase. - Part IV: Subunit composition and assembly of mitochondrial complex I. - 10. The assembly of human complex I. - 11. Complexes I in the green lineage. -Part V: Supercomplexes in mitochondria. - 12. Supramolecular organization of the respiratory chain.
Textul de pe ultima copertă
Complex I (NADH:ubiquinone oxidoreductase) is the first and largest enzyme of the respiratory chain in mitochondria and plays a central role in cellular energy production. Complex I dysfunction has been implicated in many human neurodegenerative diseases, including Parkinson’s.
Mutations in complex I subunits are among the most common human genetic disorders known. Until recently, in the absence of structural information, complex I was the least understood enzyme of the respiratory chain. The mechanism by which it couples electron transfer between NADH and quinone to the translocation of protons across the membrane was a complete enigma.
Recent years have been marked by spectacular progress in the elucidation of complex I’s structure, finally allowing the interpretation of a wealth of data accumulated in about 50 years since the discovery of the enzyme. Understanding of the mechanism of this large molecular machine, involving long-range conformational changes, is beginning to emerge.
This book is the first devoted entirely to complex I. It contains chapters written by leaders in the field, covering a wide range of topics from the structure of the complex, properties of its many redox centers, subunit composition, mutagenesis studies, evolution of the enzyme and on to the current understanding of the coupling mechanism and the molecular basis for human pathologies.
Features:
- Concise and authoritative review of current state-of-the-art in research on respiratory complex I
- The first book entirely devoted to complex I, a central enzyme in bioenergetics
- Recent breakthroughs in structure elucidation finally allow understanding of the mechanism
- Mutations leading to common and severe human disorders are discussed.
Mutations in complex I subunits are among the most common human genetic disorders known. Until recently, in the absence of structural information, complex I was the least understood enzyme of the respiratory chain. The mechanism by which it couples electron transfer between NADH and quinone to the translocation of protons across the membrane was a complete enigma.
Recent years have been marked by spectacular progress in the elucidation of complex I’s structure, finally allowing the interpretation of a wealth of data accumulated in about 50 years since the discovery of the enzyme. Understanding of the mechanism of this large molecular machine, involving long-range conformational changes, is beginning to emerge.
This book is the first devoted entirely to complex I. It contains chapters written by leaders in the field, covering a wide range of topics from the structure of the complex, properties of its many redox centers, subunit composition, mutagenesis studies, evolution of the enzyme and on to the current understanding of the coupling mechanism and the molecular basis for human pathologies.
Features:
- Concise and authoritative review of current state-of-the-art in research on respiratory complex I
- The first book entirely devoted to complex I, a central enzyme in bioenergetics
- Recent breakthroughs in structure elucidation finally allow understanding of the mechanism
- Mutations leading to common and severe human disorders are discussed.
Caracteristici
Concise review of current state-of-the-art in research on respiratory complex I The first book entirely devoted to complex I, a central enzyme in bioenergetics Recent breakthroughs in structure elucidation finally allow some understanding of the mechanism Mutations leading to common and severe human disorders are discussed