LIGHT-INDUCED OXIDATION OF IRON ATOMS IN A PHOTOSENSITIVE NITRILE HYDRATASE

被引：21

作者：

HONDA, J

TERATANI, Y

KOBAYASHI, Y

NAGAMUNE, T

SASABE, H

HIRATA, A

AMBE, F

ENDO, I

机构：

[1] INST PHYS & CHEM RES,CHEM ENGN LAB,WAKO,SAITAMA 35101,JAPAN

[2] INST PHYS & CHEM RES,FRONTIER RES PROGRAM,WAKO,SAITAMA 35101,JAPAN

[3] WASEDA UNIV,SCH SCI & ENGN,SHINJUKU KU,TOKYO 169,JAPAN

[4] INST PHYS & CHEM RES,NUCL CHEM LAB,WAKO,SAITAMA 35101,JAPAN

来源：

FEBS LETTERS | 1992年 / 301卷 / 02期

关键词：

NITRILE HYDRATASE; MOSSBAUER SPECTROSCOPY; MAGNETIC SUSCEPTIBILITY; PHOTOACTIVATION; OXIDATION; NONHEME IRON;

D O I：

10.1016/0014-5793(92)81242-E

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：

The photoactivation process of a photosensitive nitrile hydratase (NHase) from Rhodococcus sp. N-771 has been investigated by Fe-57 Mossbauer spectroscopy and magnetic susceptibility measurements in order to clarify the behavior of iron atoms in the enzyme. Mossbauer spectra of inactive NHase gave two symmetric-doublet components indicating the presence of two iron species, while that of the active NHase gave a single symmetric doublet indicating the presence of a single iron species. Magnetic susceptibility measurements of the inactive and active HNase both showed small effective magnetic moments. These results led us to conclude that one of the two iron atoms incorporated in the HNase is oxidized during photoactivation, namely from a low spin ferrous to a low ferric state. This is the first observation of an intramolecular photooxidation phenomena involving iron in a single protein molecule.

引用

页码：177 / 180

页数：4

共 11 条

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