DYNAMIC PROTEIN STRUCTURES - INFRARED EVIDENCE FOR 4 DISCRETE RAPIDLY INTERCONVERTING CONFORMERS AT THE CARBON-MONOXIDE BINDING-SITE OF BOVINE HEART MYOGLOBIN
DYNAMIC PROTEIN STRUCTURES - INFRARED EVIDENCE FOR 4 DISCRETE RAPIDLY INTERCONVERTING CONFORMERS AT THE CARBON-MONOXIDE BINDING-SITE OF BOVINE HEART MYOGLOBIN
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DOI:
10.1073/pnas.78.5.2903
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发表时间:
1981-01-01
期刊:
影响因子:
--
通讯作者:
TUCKER, MP
中科院分区:
文献类型:
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作者:
CAUGHEY, WS;SHIMADA, H;TUCKER, MP
IR spectra for the CM complex with myoglobin [Mb] isolated as the oxygenyl species from bovine heart muscle were carefully examined in the C-O stretch region as either the pH or the temperature was varied. Deconvolutions of these spectra into bands of Gaussian shape suggest the presence of 4 bands near 1938(I), 1944(II), 1954(III) and 1965(IV) cm-1 with halfband widths of about 18, 9, 9 and 10 cm-1, respectively. The relative intensities of the 4 bands varied with changes in pH or temperature. 13C NMR spectra and other evidence indicate that the 4 C.sbd.O stretch bands arise from 4 discrete rapidly interconverting conformers: CI, CII, CIII and CIV. Under conditions of physiological pH and temperature, the relative stabilities are CI .apprxeq. CII .mchgt. CIII .apprxeq. CIV. The .DELTA.H and .DELTA.S values for conformer interconversions are estimated to range from -8 to 34 kJ/mol and -27 to 87 J.cntdot.mol-1 K-1, respectively; the structures of the conformers may vary significantly. These findings provide evidence for a highly flexible, dynamic structure at the ligand-binding site of bovine myoglobin, even when ligands are bound.