1N15

FOLLOWING THE C HEME REDUCTION IN NITRITE REDUCTASE FROM PSEUDOMONAS AERUGINOSA

1N15 の概要

• エントリーDOI: 10.2210/pdb1n15/pdb
• 分子名称: NITRITE REDUCTASE, HEME C, HEME D (3 entities in total)
• 機能のキーワード: nitrite reductase, pseudomonas aeruginosa, hemoprotein, denitrification, conformational change, oxidoreductase, microspectrophotometry
• 由来する生物種: Pseudomonas aeruginosa
• 細胞内の位置: Periplasm: P24474
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 123180.08

構造登録者

Nurizzo, D.,Tegoni, M.,Cambillau, C. (登録日: 1998-09-04, 公開日: 1999-06-15, 最終更新日: 2024-04-03)

主引用文献

Nurizzo, D.,Cutruzzola, F.,Arese, M.,Bourgeois, D.,Brunori, M.,Cambillau, C.,Tegoni, M.
Does the reduction of c heme trigger the conformational change of crystalline nitrite reductase?
J.Biol.Chem., 274:14997-15004, 1999

PubMed Abstract: The structures of nitrite reductase from Paracoccus denitrificans GB17 (NiR-Pd) and Pseudomonas aeruginosa (NiR-Pa) have been described for the oxidized and reduced state (Fülöp, V., Moir, J. W. B., Ferguson, S. J., and Hajdu, J. (1995) Cell 81, 369-377; Nurizzo, D., Silvestrini, M. C., Mathieu, M., Cutruzzolà, F., Bourgeois, D., Fülöp, V., Hajdu, J., Brunori, M., Tegoni, M., and Cambillau, C. (1997) Structure 5, 1157-1171; Nurizzo, D., Cutruzzolà, F., Arese, M., Bourgeois, D., Brunori, M., Cambillau, C. , and Tegoni, M. (1998) Biochemistry 37, 13987-13996). Major conformational rearrangements are observed in the extreme states although they are more substantial in NiR-Pd. The four structures differ significantly in the c heme domains. Upon reduction, a His17/Met106 heme-ligand switch is observed in NiR-Pd together with concerted movements of the Tyr in the distal site of the d1 heme (Tyr10 in NiR-Pa, Tyr25 in NiR-Pd) and of a loop of the c heme domain (56-62 in NiR-Pa, 99-116 in NiR-Pd). Whether the reduction of the c heme, which undergoes the major rearrangements, is the trigger of these movements is the question addressed by our study. This conformational reorganization is not observed in the partially reduced species, in which the c heme is partially or largely (15-90%) reduced but the d1 heme is still oxidized. These results suggest that the d1 heme reduction is likely to be responsible of the movements. We speculate about the mechanistic explanation as to why the opening of the d1 heme distal pocket only occurs upon electron transfer to the d1 heme itself, to allow binding of the physiological substrate NO2- exclusively to the reduced metal center.

PubMed: 10329702
DOI: 10.1074/jbc.274.21.14997

実験手法

X-RAY DIFFRACTION (2.9 Å)