Enzyme-like effect of metmyoglobin on the thermal cis-trans isomerization of stilbazolium betaine.
A photochromic compound, stilbazolium betaine M, when associated with metmyoglobin undergoes an accelerated thermal cis-trans isomerization. A study of the pH and ionic strength dependence of the isomerization reaction rate of the photochrome associated with metmyoglobin was performed. A comparative investigation of the reaction carried out in the presence of three proteins, metmyoglobin, apomyoglobin, and human albumin, indicates a specific influence of the heme pocket environment on the reaction. Possible mechanisms of the reaction acceleration are considered.
Pastukhov
A V
AV
Institute of Problems of Chemical Physics, Russian Academy of Sciences, Chernogolovka, Moscow region. pastukh@cat.icp.ac.ru
Vogel
V R
VR
Kotelnikov
A I
AI
D000418:Albumins / Q000378:metabolism; D001059:Apoproteins / Q000378:metabolism; D001597:Benzylidene Compounds / Q000737:chemistry / Q000378:metabolism*; D002384:Catalysis; D004095:Dihydropyridines / Q000737:chemistry / Q000378:metabolism*; D006418:Heme / Q000737:chemistry; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D008786:Metmyoglobin / Q000378:metabolism*; D008961:Models, Structural; D009211:Myoglobin / Q000378:metabolism; D009994:Osmolar Concentration; D013237:Stereoisomerism; D013696:Temperature
D000418:Albumins; D001059:Apoproteins; D001597:Benzylidene Compounds; D004095:Dihydropyridines; D009211:Myoglobin; C010857:apomyoglobin; C095319:stilbazolium merocyanine; D008786:Metmyoglobin; D006418:Heme