COMBINING MOSSBAUER-SPECTROSCOPY WITH INTEGER SPIN ELECTRON-PARAMAGNETIC-RESONANCE

被引:58
作者
MUNCK, E [1 ]
SURERUS, KK [1 ]
HENDRICH, MP [1 ]
机构
[1] UNIV MINNESOTA,DEPT CHEM,MINNEAPOLIS,MN 55455
来源
METALLOBIOCHEMISTRY, PT D | 1993年 / 227卷
关键词
D O I
10.1016/0076-6879(93)27019-D
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Integer spin EPR will become an important tool for the studies of the active sites of iron-containing metalloproteins. Laboratories have focused on combined EPR and Mössbauer studies of systems yielding Mössbauer spectra that could be analyzed with high accuracy and confidence in the framework of the spin Hamiltonian formalism. Using zerofield splitting parameters from the Mössbauer analysis, it is possible to assign EPR transitions with confidence and refine the methods of EPR data analysis. Integer spin EPR, in turn, has aided in recognizing the fundamental features of some systems; in particular, it has helped to solve the problem of the P cluster state pox. Some of the iron-containing proteins and model complexes for which integer spin EPR has been observed are presented in the chapter. A survey of the literature on Mössbauer spectroscopy suggests that a variety of other iron-containing proteins are likely to exhibit integer spin EPR at either X- or Q-band frequencies. Based on the progress that has been made in the past it is anticipated that this technique will be a valuable tool for the biochemist and biophysicist. By applying Mössbauer and EPR spectroscopy to proteins with multiple iron-containing sites and using the methodology discussed above, one should be able to untangle quite complex situations. © 1993, Elsevier Inc. All rights reserved.
引用
收藏
页码:463 / 479
页数:17
相关论文
共 18 条
[1]   FE(II)-SUBSTITUTED HORSE LIVER ALCOHOL-DEHYDROGENASE, A MODEL FOR NON-HEME IRON ENZYMES - VARIOUS STATES OF IRON-DIOXYGEN INTERACTION INVESTIGATED BY MOSSBAUER AND EPR SPECTROSCOPY [J].
BILL, E ;
HAAS, C ;
DING, XQ ;
MARET, W ;
WINKLER, H ;
TRAUTWEIN, AX ;
ZEPPEZAUER, M .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1989, 180 (01) :111-121
[2]   MODELS FOR DIFERROUS FORMS OF IRON-OXO PROTEINS - STRUCTURE AND PROPERTIES OF [FE2BPMP(O2CR)2]BPH4 COMPLEXES [J].
BOROVIK, AS ;
HENDRICH, MP ;
HOLMAN, TR ;
MUNCK, E ;
PAPAEFTHYMIOU, V ;
QUE, L .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1990, 112 (16) :6031-6038
[3]  
CHRISTNER JA, 1981, J BIOL CHEM, V256, P2098
[4]  
EMPTAGE MH, 1980, J BIOL CHEM, V255, P1793
[5]   MOSSBAUER, EPR, AND ENDOR STUDIES OF THE HYDROXYLASE AND REDUCTASE COMPONENTS OF METHANE MONOOXYGENASE FROM METHYLOSINUS-TRICHOSPORIUM OB3B [J].
FOX, BG ;
HENDRICH, MP ;
SURERUS, KK ;
ANDERSSON, KK ;
FROLAND, WA ;
LIPSCOMB, JD ;
MUNCK, E .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1993, 115 (09) :3688-3701
[7]   ELECTRON-PARAMAGNETIC-RES SPECTRA OF QUINTET FERROUS MYOGLOBIN AND A MODEL HEME COMPOUND [J].
HENDRICH, MP ;
DEBRUNNER, PG .
JOURNAL OF MAGNETIC RESONANCE, 1988, 78 (01) :133-141
[8]   INTEGER-SPIN EPR STUDIES OF THE FULLY REDUCED METHANE MONOOXYGENASE HYDROXYLASE COMPONENT [J].
HENDRICH, MP ;
MUNCK, E ;
FOX, BG ;
LIPSCOMB, JD .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1990, 112 (15) :5861-5865
[9]   MULTIFIELD SATURATION MAGNETIZATION AND MULTIFREQUENCY EPR MEASUREMENTS OF DEOXYHEMERYTHRIN AZIDE - A UNIFIED PICTURE [J].
HENDRICH, MP ;
PEARCE, LL ;
QUE, L ;
CHASTEEN, ND ;
DAY, EP .
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY, 1991, 113 (08) :3039-3044
[10]   INTEGER-SPIN ELECTRON-PARAMAGNETIC RESONANCE OF IRON PROTEINS [J].
HENDRICH, MP ;
DEBRUNNER, PG .
BIOPHYSICAL JOURNAL, 1989, 56 (03) :489-506