Electrochemical and spectroscopic properties of the iron-sulfur flavoprotein from Methanosarcina thermophila

被引:16
作者
Becker, DF
Leartsakulpanich, U
Surerus, KK
Ferry, JG
Ragsdale, SW [1 ]
机构
[1] Univ Nebraska, Beadle Ctr, Dept Biochem, Lincoln, NE 68588 USA
[2] Penn State Univ, Eberly Coll Sci, Dept Biochem & Mol Biol, University Pk, PA 16802 USA
[3] Univ Wisconsin, Dept Chem, Milwaukee, WI 53201 USA
关键词
D O I
10.1074/jbc.273.41.26462
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
An iron-sulfur flavoprotein (Isf) from the methanoarchaeaon Methanosarcina thermophila, which participates in electron transfer reactions required for the fermentation of acetate to methane, was characterized by electrochemistry and EPR and Mossbauer spectroscopy. The midpoint potential (E-m) of the FMN/FMNH2 couple was -0.277 V. No flavin semiquinone was observed during potentiometric titrations; however, low amounts of the radical were observed when Isf was quickly frozen after reaction with CO and the CO dehydrogenase/acetyl-CoA synthase complex from M. thermophila. Isf contained a [4Fe-4S](2+/1+) cluster with g values of 2.06 and 1.93 and an unusual split signal with g values at 1.86 and 1.82. The unusual morphology was attributed to microheterogeneity among Isf molecules. The E-m value for the 2+/1+ redox couple of the cluster was -0.394 V, Extracts from H-2-CO2-grown Methanobacterium thermoautotrophicum cells catalyzed either the H-2- or CO-dependent reduction of M. thermophila Isf, In addition, Isf homologs were found in the genomic sequences of the CO2-reducing methanoarchaea M. thermoautotrophicum and Methanococcus jannaschii. These results support a general role for Isf in electron transfer reactions of both acetate-fermenting and CO2-reducing methanoarchaea, It is suggested that Isf functions to couple electron transfer from ferredoxin to membrane-bound electron carriers, such as methanophenazine and/or b-type cytochromes.
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页码:26462 / 26469
页数:8
相关论文
共 43 条
[1]   Isolation and characterization of methanophenazine and function of phenazines in membrane-bound electron transport of Methanosarcina mazei Gol [J].
Abken, HJ ;
Tietze, M ;
Brodersen, J ;
Bäumer, S ;
Beifuss, U ;
Deppenmeier, U .
JOURNAL OF BACTERIOLOGY, 1998, 180 (08) :2027-2032
[2]   PURIFICATION AND PROPERTIES OF THE MEMBRANE-ASSOCIATED COENZYME F420-REDUCING HYDROGENASE FROM METHANOBACTERIUM-FORMICICUM [J].
BARON, SF ;
FERRY, JG .
JOURNAL OF BACTERIOLOGY, 1989, 171 (07) :3846-3853
[3]  
BONAM D, 1987, J BIOL CHEM, V262, P2980
[4]   STRUCTURE, FUNCTION AND EVOLUTION OF BACTERIAL FERREDOXINS [J].
BRUSCHI, M ;
GUERLESQUIN, F .
FEMS MICROBIOLOGY LETTERS, 1988, 54 (02) :155-175
[5]   Complete genome sequence of the methanogenic archaeon, Methanococcus jannaschii [J].
Bult, CJ ;
White, O ;
Olsen, GJ ;
Zhou, LX ;
Fleischmann, RD ;
Sutton, GG ;
Blake, JA ;
FitzGerald, LM ;
Clayton, RA ;
Gocayne, JD ;
Kerlavage, AR ;
Dougherty, BA ;
Tomb, JF ;
Adams, MD ;
Reich, CI ;
Overbeek, R ;
Kirkness, EF ;
Weinstock, KG ;
Merrick, JM ;
Glodek, A ;
Scott, JL ;
Geoghagen, NSM ;
Weidman, JF ;
Fuhrmann, JL ;
Nguyen, D ;
Utterback, TR ;
Kelley, JM ;
Peterson, JD ;
Sadow, PW ;
Hanna, MC ;
Cotton, MD ;
Roberts, KM ;
Hurst, MA ;
Kaine, BP ;
Borodovsky, M ;
Klenk, HP ;
Fraser, CM ;
Smith, HO ;
Woese, CR ;
Venter, JC .
SCIENCE, 1996, 273 (5278) :1058-1073
[6]  
CHRISTNER JA, 1983, J BIOL CHEM, V258, P1157
[7]   CHARACTERIZATION OF THE IRON-SULFUR CLUSTERS IN FERREDOXIN FROM ACETATE-GROWN METHANOSARCINA-THERMOPHILA [J].
CLEMENTS, AP ;
KILPATRICK, L ;
LU, WP ;
RAGSDALE, SW ;
FERRY, JG .
JOURNAL OF BACTERIOLOGY, 1994, 176 (09) :2689-2693
[8]   CARBON-MONOXIDE OXIDATION BY METHANOGENIC BACTERIA [J].
DANIELS, L ;
FUCHS, G ;
THAUER, RK ;
ZEIKUS, JG .
JOURNAL OF BACTERIOLOGY, 1977, 132 (01) :118-126
[9]   INACTIVATION OF YEAST ENOLASE BY 2,3-BUTANEDIONE [J].
ELLIOTT, JI ;
BREWER, JM .
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 1978, 190 (01) :351-357
[10]  
Ferry JamesG., 2012, METHANOGENESIS ECOLO