ACTIVE-SITE ANALYSIS OF FERRIC P450 ENZYMES - HYDROGEN-BONDING EFFECTS ON THE CIRCULAR-DICHROISM SPECTRA

被引：32

作者：

ANDERSSON, LA ^{[1
]}

PETERSON, JA ^{[1
]}

机构：

[1] UNIV TEXAS, SW MED CTR, DEPT BIOCHEM, DALLAS, TX 75235 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1995年 / 211卷 / 02期

关键词：

D O I：

10.1006/bbrc.1995.1826

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Active-site CD spectra were analyzed for P450's with known x-ray structures (P450terp, P450BM-3, P450cam). CD spectral patterns for Fe3+-substrate-free P450's reflect structure/function properties of the distal pocket. P450terp and P450BM-3 have an H-bond between 6th ligand and I-helix [Hasemann, C.A., et al. (1995) Structure, 3, 41-62], and the Soret CD band at similar to 410 nm is similar to 2-fold larger than that at similar to 350 nm. For P450cam, the two CD bands are more nearly equal, and the 6th ligand is not H-bonded to the I-helix. The CD spectral pattern can be used to predict active-site structural properties, e.g., H-bonding and polarity. (C) 1995 Academic Press, Inc.

引用

页码：389 / 395

页数：7

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