Temperature dependence of Q-band electron paramagnetic resonance spectra of nitrosyl heme proteins

被引：20

作者：

Flores, M ^{[1
]}

Wajnberg, E ^{[1
]}

Bemski, G ^{[1
]}

机构：

[1] CTR BRASILEIRO PESQUISAS FIS,BR-22290180 RIO JANEIRO,BRAZIL

来源：

BIOPHYSICAL JOURNAL | 1997年 / 73卷 / 06期

关键词：

D O I：

10.1016/S0006-3495(97)78347-4

中图分类号：

Q6 [生物物理学];

学科分类号：

071011 ;

摘要：

The Q-band (35 GHz) electron paramagnetic resonance (EPR) spectra of nitrosyl hemoglobin (HbNO) and nitrosyl myoglobin (MbNO) were studied as a function of temperature between 19 K and 200 K. The spectra of both heme proteins show two classes of variations as a function of temperature. The first one has previously been associated with the existence of two paramagnetic species, one with rhombic and the other with axial symmetry. The second one manifests itself in changes in the g-factors and linewidths of each species. These changes are correlated with the conformational substates model and associate the variations of g-values with changes in the angle of the N(his)-Fe-N(NO) bond in the rhombic species and with changes in the distance between Fe and N of the proximal (F8) histidine in the axial species.

引用

页码：3225 / 3229

页数：5

共 24 条

[1] CONFORMATIONAL RELAXATION AND LIGAND-BINDING IN MYOGLOBIN [J].

ANSARI, A ;

JONES, CM ;

HENRY, ER ;

HOFRICHTER, J ;

EATON, WA .

BIOCHEMISTRY, 1994, 33 (17) :5128-5145

[2] DYNAMICS OF LIGAND-BINDING TO MYOGLOBIN [J].

AUSTIN, RH ;

BEESON, KW ;

EISENSTEIN, L ;

FRAUENFELDER, H ;

GUNSALUS, IC .

BIOCHEMISTRY, 1975, 14 (24) :5355-5373

[3]

Belford R. L., 1979, EPR S 21 ROCK MOUNT

[4]

BIZARRI AR, 1993, EUR BIOPHYS J, V22, P259

[5] AN ELECTRON-SPIN-RESONANCE STUDY OF NITROSYL APLYSIA-BRASILIANA MYOGLOBIN AND NITROSYL ANNELIDAE GLOSSOSCOLEX-PAULISTUS ERYTHROCRUORIN [J].

CARACELLI, I ;

MEIRELLES, NC ;

TABAK, M ;

BAFFA, O ;

NASCIMENTO, OR .

BIOCHIMICA ET BIOPHYSICA ACTA, 1988, 955 (03) :315-320

[6] ANALOGOUS EFFECT OF PROTONS AN INOSITOL HEXAPHOSPHATE ON ALTERATION OF STRUCTURE OF NITROSYL FETAL HUMAN HEMOGLOBIN [J].

CHEVION, M ;

STERN, A ;

PEISACH, J ;

BLUMBERG, WE ;

SIMON, S .

BIOCHEMISTRY, 1978, 17 (09) :1745-1750

[7]

CUPANE A, 1993, EUR BIOPHYS J BIOPHY, V21, P385, DOI 10.1007/BF00185865

[8] THE ENERGY LANDSCAPES AND MOTIONS OF PROTEINS [J].

FRAUENFELDER, H ;

SLIGAR, SG ;

WOLYNES, PG .

SCIENCE, 1991, 254 (5038) :1598-1603

[9] ELECTRON-PARAMAGNETIC STUDIES OF NITRIC-OXIDE HEMOGLOBIN DERIVATIVES - ISOLATED SUBUNITS AND NITRIC-OXIDE HYBRIDS [J].

HENRY, Y ;

BANERJEE, R .

JOURNAL OF MOLECULAR BIOLOGY, 1973, 73 (04) :469-482

[10] METASTABILITY OF THE FOLDED STATES OF GLOBULAR-PROTEINS [J].

HONEYCUTT, JD ;

THIRUMALAI, D .

PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1990, 87 (09) :3526-3529

← 1 2 3 →