Participation of carboxylate amino acid side chain in regiospecific oxidation of heme by heme oxygenase [7]

Journal of the American Chemical Society

Volumn 122, Issue 34, 2000, Pages 8311-8312

  Zhou, Hong ^a,f   Migita, Catharina Taiko ^b   Sato, Michihiko ^a   Sun, Danyu ^a   Zhang, Xuhong ^a   Ikeda Saito, Masao ^c,d   Fujii, Hiroshi ^e   Yoshida, Tadashi ^a  

^a YAMAGATA UNIVERSITY   (Japan)

^b YAMAGUCHI UNIVERSITY   (Japan)

^c CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

^d TOHOKU UNIVERSITY   (Japan)

^e INSTITUTE FOR MOLECULAR SCIENCE   (Japan)

^f HARBIN MEDICAL UNIVERSITY   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACID; CARBOXYLIC ACID DERIVATIVE; HEME OXYGENASE; PROPIONIC ACID;

CATALYSIS; HYDROGEN BOND; LETTER; OXIDATION; REACTION ANALYSIS; SITE DIRECTED MUTAGENESIS; STEREOCHEMISTRY;

EID: 0034734346     PISSN: 00027863     EISSN: None     Source Type: Journal    
DOI: 10.1021/ja0002868     Document Type: Letter

References (14)

1. Tenhunen, R.; Marver, H. S.; Schmid, R. J. Biol. Chem. 1969, 244, 6388-6394.
2. (a) Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1978, 253, 4224-4229.
3. (b) Yoshida, T.; Kikuchi, G. J. Biol. Chem. 1979, 254, 4487-4491.
4. Maines, M. D. FASEB J. 1988, 2, 2557-2568.
5. Maines, M. D. In Heme Oxygenase-Clinical Applications and Functions; CRC Press: Boca Raton, FL, 1992.
6. (a) Lemberg, R. Cortis-Jones, B.; Norrie, M. Nature, 1937,139, 1016.
7. (b) Bonnett, R.; McDonagh, A. F. J. Chem. Soc., Perkin Trans. 1 1973, 881-888.
8. Schuller, D. J.; Wilks, A.; Oritz de Montellano, P. R.; Poulos, T. L. Nat. Struct. Biol. 1999, 6, 860-867.
9. (a)Takahashi, S.; Wang, J.; Rousseau, D. L.; Ishikawa, K.; Yoshida, T.; Host, J. R.; Ikeda-Saito, M. J. Biol. Chem. 1994, 269, 1010-1014.
10. (b) Sun, J.; Wilks, A.; Oritz de Montellano, P. R.; Loehr, T. M. Biochemistry 1993, 32, 14151-14157.
11. R183E- and R183D-HO could degrade heme to biliverdin with NADPH and NADPH-cytochrome P450 reductase, but the reactions were much slower than those of the wild-type complex. The electron transfer rate from the reductase is drastically decreased for R183E and R183D, but not for R183N, R183A, R183Y, and R183T (See Supporting Information). The electronic repulsion formed by the negative charge introduced at position 183 in R183E and R183D would weaken the interaction with the reductase and decrease in electron-transfer rate.
12. Rotenberg, M. O.; Maines, M. D. Arch. Biochem. Biophys. 1991, 290, 336-344.
13. As observed for the wild-type complex, heme-R183D and -R183E complexes exhibit two sets of heme methyl signals due to the heme orientational disorder (isomer X and Y). Interestingly, the heme methyl signals of the isomer X are significantly broadened than those of the isomer Y and the wild-type complex. This appears to indicate that heme of the isomer X rapidly fluctuates due to the electronic repulsion of the carboxylates in R183D and R183E, and this fluctuation may change the regioselectivity.
14. a of 7.9, respectively.