CYANIDE DISSOCIATION FROM THE HEMOGLOBIN OF PARASCARIS-EQUORUM

被引:7
作者
ANTONINI, G
BELLELLI, A
CONCETTI, A
FALCIONI, G
BRUNORI, M
机构
[1] UNIV ROMA LA SAPIENZA,DEPT BIOCHEM SCI,I-00185 ROME,ITALY
[2] UNIV ROMA LA SAPIENZA,CNR,CTR MOLEC BIOL,I-00185 ROME,ITALY
[3] UNIV ROMA TOR VERGATA,DEPT EXPTL MED & BIOCHEM SCI,I-00100 ROME,ITALY
[4] UNIV CAMERINO,DEPT CELL BIOL,I-62032 CAMERINO,ITALY
来源
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 1994年 / 1205卷 / 02期
关键词
HEMOGLOBIN; LIGAND BINDING; TRANSIENT SPECTROSCOPY; SVD ANALYSIS; (P-EQUORUM);
D O I
10.1016/0167-4838(94)90241-0
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 reduction of cyanomethemoglobin by dithionite leads to the appearance of an intermediate, the complex of cyanide with ferrous hemoglobin, whose dissociation is easily followed in a stopped flow apparatus. This reaction was studied in the hemoglobin from the parasitic nematode Parascaris equorum, whose extremely high oxygen affinity is due to a very low dissociation rate. The rate of cyanide dissociation from ferrous Parascaris hemoglobin is not so dramatically different from that of other hemoglobins and myoglobins. Other features of the reaction are: (i) the rate constant of cyanide release is pH independent, an observation which is agreement with the possible absence of the distal histidine, given the mechanism suggested in a previous study (Bellelli, A., Antonini, G., Brunori, M, Springer, B.A. and Sligar, S.G. (1990) J. Biol. Chem. 265, 18898-18901), and (ii) the time-course shows no kinetic cooperativity. The structural basis of the extremely high oxygen affinity of Parascaris hemoglobin cannot be explained on the basis of the results here reported. This study also confirms that, even though cyanide binding to ferrous hemoglobins is controlled by distal interactions, the functional behaviour of this ligand is characteristic and differs from the behaviour of oxygen.
引用
收藏
页码:252 / 257
页数:6
相关论文
共 21 条
[1]  
ANTONINI E, 1971, HEMOGLOBIN MYOGLOBIN
[2]  
BELLELLI A, 1990, J BIOL CHEM, V265, P18898
[3]   X-RAY CRYSTAL-STRUCTURE OF THE FLUORIDE DERIVATIVE OF APLYSIA-LIMACINA FERRIC MYOGLOBIN AT 2.0 A RESOLUTION - STABILIZATION OF THE FLUORIDE-ION BY HYDROGEN-BONDING TO ARG66 (E10) [J].
BOLOGNESI, M ;
CODA, A ;
FRIGERIO, F ;
GATTI, G ;
ASCENZI, P ;
BRUNORI, M .
JOURNAL OF MOLECULAR BIOLOGY, 1990, 213 (04) :621-625
[4]  
BRUNORI M, 1992, J BIOL CHEM, V267, P2258
[5]   LIGAND-DEPENDENT BEHAVIOR OF THE HEMOGLOBIN FROM THE ASCARID PARASCARIS-EQUORUM [J].
COLETTA, M ;
FALCIONI, G ;
CONCETTI, A ;
ASCOLI, F ;
BRUNORI, M .
BIOCHIMICA ET BIOPHYSICA ACTA, 1986, 870 (01) :169-175
[6]   REDUCTION BY DITHIONITE OF FE(III) MYOGLOBIN DERIVATIVES WITH DIFFERENT LIGANDS ATTACHED TO IRON ATOM - STUDY BY RAPID-WAVELENGTH-SCANNING STOPPED-FLOW SPECTROPHOTOMETRY [J].
COX, RP ;
HOLLAWAY, MR .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1977, 74 (03) :575-587
[7]   REACTION OF FE(III) MYOGLOBIN FLUORIDE WITH REDUCING AGENTS [J].
COX, RP .
BIOCHEMICAL JOURNAL, 1977, 167 (02) :493-495
[8]   QUATERNARY STRUCTURE OF ERYTHROCRUORIN FROM THE NEMATODE ASCARIS-SUUM - EVIDENCE FOR UNSATURATED HEME-BINDING SITES [J].
DARAWSHE, S ;
TSAFADYAH, Y ;
DANIEL, E .
BIOCHEMICAL JOURNAL, 1987, 242 (03) :689-694
[9]   POLAR ZIPPER SEQUENCE IN THE HIGH-AFFINITY HEMOGLOBIN OF ASCARIS-SUUM - AMINO-ACID-SEQUENCE AND STRUCTURAL INTERPRETATION [J].
DEBAERE, I ;
LIU, L ;
MOENS, L ;
VANBEEUMEN, J ;
GIELENS, C ;
RICHELLE, J ;
TROTMAN, C ;
FINCH, J ;
GERSTEIN, M ;
PERUTZ, M .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1992, 89 (10) :4638-4642
[10]  
DEBAERE I, 1991, STRUCTURE AND FUNCTION OF INVERTEBRATE OXYGEN CARRIERS, P271