Intermediates formed by the Co2+-activated ribulose-1,5-bisphosphate carboxylase/oxygenase from spinach studied by electron paramagnetic resonance spectroscopy.
Two enzyme-metal-bound intermediates formed by the Co2+-activated ribulose-1,5-bisphosphate carboxylase/oxygenase (EC 4.1.1.39) have been studied by electron paramagnetic resonance (EPR) spectroscopy. Their rates of approach to a stationary state are different and their relative amounts at steady state are dependent on the concentration of ribulose 1,5-bisphosphate. It is therefore proposed that enzyme-metal-coordinated ribulose 1,5-bisphosphate and an enzyme-metal-coordinated enediolate anion of it, where bound ribulose 1,5-bisphosphate appears first, constitute the two EPR-detectable intermediates, respectively.
Brändén
R
R
Department of Biochemistry and Biophysics, University of Göteborg, Sweden.
Janson
K
K
Nilsson
P
P
Aasa
R
R
D003035:Cobalt / Q000378:metabolism*; D004578:Electron Spin Resonance Spectroscopy; D010944:Plants / Q000201:enzymology*; D012273:Ribulose-Bisphosphate Carboxylase / Q000378:metabolism*; D012274:Ribulosephosphates / Q000378:metabolism
D012274:Ribulosephosphates; C001933:ribulose-1,5 diphosphate; D003035:Cobalt; D012273:Ribulose-Bisphosphate Carboxylase