2N9J

Solution structure of oxidized human cytochrome c

Summary for 2N9J

• Entry DOI: 10.2210/pdb2n9j/pdb
• Related: 2N9I
• NMR Information: BMRB: 25908
• Descriptor: Cytochrome c, HEME C (2 entities in total)
• Functional Keywords: cytochrome c, electron transfer, electron transport
• Biological source: Homo sapiens (human)
• Cellular location: Mitochondrion intermembrane space: P99999
• Total number of polymer chains: 1
• Total formula weight: 12259.09

Authors

Imai, M.,Saio, T.,Kumeta, H.,Uchida, T.,Inagaki, F.,Ishimori, K. (deposition date: 2015-11-24, release date: 2016-02-17, Last modification date: 2024-11-06)

Primary citation

Imai, M.,Saio, T.,Kumeta, H.,Uchida, T.,Inagaki, F.,Ishimori, K.
Investigation of the redox-dependent modulation of structure and dynamics in human cytochrome c.
Biochem.Biophys.Res.Commun., 469:978-984, 2016

PubMed Abstract: Redox-dependent changes in the structure and dynamics of human cytochrome c (Cyt c) were investigated by solution NMR. We found significant structural changes in several regions, including residues 23-28 (loop 3), which were further corroborated by chemical shift differences between the reduced and oxidized states of Cyt c. These differences are essential for discriminating redox states in Cyt c by cytochrome c oxidase (CcO) during electron transfer reactions. Carr-Purcell-Meiboom-Gill (CPMG) relaxation dispersion experiments identified that the region around His33 undergoes conformational exchanges on the μs-ms timescale, indicating significant redox-dependent structural changes. Because His33 is not part of the interaction site for CcO, our data suggest that the dynamic properties of the region, which is far from the interaction site for CcO, contribute to conformational changes during electron transfer to CcO.

PubMed: 26718409
DOI: 10.1016/j.bbrc.2015.12.079

Experimental method

SOLUTION NMR