Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain

L.A. Sazanov, Biochemistry 46 (2007) 2275–2288.

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Abstract
Complex I of respiratory chains plays a central role in cellular energy production. Mutations in its subunits lead to many human neurodegenerative diseases. Recently, a first atomic structure of the hydrophilic domain of complex I from Thermus thermophilus was determined. This domain represents a catalytic core of the enzyme. It consists of eight different subunits, contains all the redox centers, and comprises more than half of the entire complex. In this review, novel mechanistic implications of the structure are discussed, and the effects of many known mutations of complex I subunits are interpreted in a structural context.
Publishing Year
Date Published
2007-03-06
Journal Title
Biochemistry
Volume
46
Issue
9
Page
2275 - 2288
IST-REx-ID

Cite this

Sazanov LA. Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. 2007;46(9):2275-2288. doi:10.1021/bi602508x
Sazanov, L. A. (2007). Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry, 46(9), 2275–2288. https://doi.org/10.1021/bi602508x
Sazanov, Leonid A. “Respiratory Complex I: Mechanistic and Structural Insights Provided by the Crystal Structure of the Hydrophilic Domain.” Biochemistry 46, no. 9 (2007): 2275–88. https://doi.org/10.1021/bi602508x.
L. A. Sazanov, “Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain,” Biochemistry, vol. 46, no. 9, pp. 2275–2288, 2007.
Sazanov LA. 2007. Respiratory complex I: Mechanistic and structural insights provided by the crystal structure of the hydrophilic domain. Biochemistry. 46(9), 2275–2288.
Sazanov, Leonid A. “Respiratory Complex I: Mechanistic and Structural Insights Provided by the Crystal Structure of the Hydrophilic Domain.” Biochemistry, vol. 46, no. 9, ACS, 2007, pp. 2275–88, doi:10.1021/bi602508x.

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