Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the heme - PubMed (original) (raw)
Comparative Study
. 2000 Feb;267(3):755-66.
doi: 10.1046/j.1432-1327.2000.01054.x.
Affiliations
- PMID: 10651812
- DOI: 10.1046/j.1432-1327.2000.01054.x
Free article
Comparative Study
Solution structure of oxidized microsomal rabbit cytochrome b5. Factors determining the heterogeneous binding of the heme
L Banci et al. Eur J Biochem. 2000 Feb.
Free article
Abstract
Cytochrome b5 is heterogeneous in solution because of the presence of two isomers (A and B), differing in the rotation of the heme plane around the axis defined by the alpha and gamma meso protons. For rabbit cytochrome b5, the A/B ratio is 5 : 1. The solution structure of the major form of the oxidized soluble fragment of rabbit microsomal cytochrome b5 (94 amino acids) is here solved through NMR spectroscopy. From 1908 NOEs, of which 1469 were meaningful, there were 246 pseudocontact shifts and 18 3J couplings, a family of 40 energy-minimized conformers were obtained with average backbone rmsd (for residues 4-84) of 0.060 +/- 0.016 nm and average target function of 0.0078 nm2, no distance violations being larger than 0.03 nm. The structure was compared with the solution structures of the A (major) and B (minor) isomers of the rat cytochrome in the oxidized form. The A/B ratio for the rat cytochrome is 1.5 : 1, despite the very high sequence similarity (93%) to the rabbit protein. This comparison has provided insights into the factors determining the distribution in solution of the two isomers differing with respect to heme orientation. It appears that residues 23 and 74 are both important in determining this distribution, through interaction of their side chains with the prosthetic group. Hydrophobic and steric interactions are the key factors in determining the relative stability of one isomer with respect to the other.
Similar articles
- Solution structure of reduced microsomal rat cytochrome b5.
Banci L, Bertini I, Ferroni F, Rosato A. Banci L, et al. Eur J Biochem. 1997 Oct 1;249(1):270-9. doi: 10.1111/j.1432-1033.1997.t01-1-00270.x. Eur J Biochem. 1997. PMID: 9363779 - Solution structure of the B form of oxidized rat microsomal cytochrome b5 and backbone dynamics via 15N rotating-frame NMR-relaxation measurements. Biological implications.
Arnesano F, Banci L, Bertini I, Felli IC, Koulougliotis D. Arnesano F, et al. Eur J Biochem. 1999 Mar;260(2):347-54. doi: 10.1046/j.1432-1327.1999.00167.x. Eur J Biochem. 1999. PMID: 10095768 - The solution structure of oxidized rat microsomal cytochrome b5.
Arnesano F, Banci L, Bertini I, Felli IC. Arnesano F, et al. Biochemistry. 1998 Jan 6;37(1):173-84. doi: 10.1021/bi971896w. Biochemistry. 1998. PMID: 9425037 - The cytochrome b5-fold: an adaptable module.
Lederer F. Lederer F. Biochimie. 1994;76(7):674-92. doi: 10.1016/0300-9084(94)90144-9. Biochimie. 1994. PMID: 7893819 Review. - NMR solution structure, backbone mobility, and homology modeling of c-type cytochromes from gram-positive bacteria.
Banci L, Bertini I, Ciurli S, Dikiy A, Dittmer J, Rosato A, Sciara G, Thompsett AR. Banci L, et al. Chembiochem. 2002 Apr 2;3(4):299-310. doi: 10.1002/1439-7633(20020402)3:4<299::AID-CBIC299>3.0.CO;2-0. Chembiochem. 2002. PMID: 11933230 Review.
Cited by
- High-resolution crystal structures of the solubilized domain of porcine cytochrome b5.
Hirano Y, Kimura S, Tamada T. Hirano Y, et al. Acta Crystallogr D Biol Crystallogr. 2015 Jul;71(Pt 7):1572-81. doi: 10.1107/S1399004715009438. Epub 2015 Jun 30. Acta Crystallogr D Biol Crystallogr. 2015. PMID: 26143928 Free PMC article. - Cellular solid-state NMR investigation of a membrane protein using dynamic nuclear polarization.
Yamamoto K, Caporini MA, Im SC, Waskell L, Ramamoorthy A. Yamamoto K, et al. Biochim Biophys Acta. 2015 Jan;1848(1 Pt B):342-9. doi: 10.1016/j.bbamem.2014.07.008. Epub 2014 Jul 11. Biochim Biophys Acta. 2015. PMID: 25017802 Free PMC article. - Shortening spin-lattice relaxation using a copper-chelated lipid at low-temperatures - A magic angle spinning solid-state NMR study on a membrane-bound protein.
Yamamoto K, Caporini MA, Im S, Waskell L, Ramamoorthy A. Yamamoto K, et al. J Magn Reson. 2013 Dec;237:175-181. doi: 10.1016/j.jmr.2013.10.017. Epub 2013 Nov 1. J Magn Reson. 2013. PMID: 24246881 Free PMC article. - ¹H, ¹³C and ¹⁵N resonance assignments for the full-length mammalian cytochrome b₅ in a membrane environment.
Vivekanandan S, Ahuja S, Im SC, Waskell L, Ramamoorthy A. Vivekanandan S, et al. Biomol NMR Assign. 2014 Oct;8(2):409-13. doi: 10.1007/s12104-013-9528-9. Epub 2013 Oct 9. Biomol NMR Assign. 2014. PMID: 24105099 Free PMC article.
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources
Molecular Biology Databases