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Papers In Press, published online ahead of print January 12, 2001
J. Biol. Chem, 10.1074/jbc.M010217200
Submitted on November 9, 2000
Revised on January 12, 2001
Accepted on January 12, 2001

The Role of Water Molecules in the Association of Cytochrome P450cam with Putidaredoxin : An Osmotic Pressure Study

Yoshiaki Furukawa and Isao Morishima

Department of Molecular Engineering, Kyoto University, Kyoto 606-8501

Corresponding Author: morisima{at}mds.moleng.kyoto-u.ac.jp

We have investigated the osmotic pressure dependence of the association between ferric cytochrome P450cam and putidaredoxin (Pdx), in order to gain an insight into the role of water molecules in the P450cam/reduced Pdx complexation amenable to the physiological electron transfer. The association constant was evaluated from the electron transfer rates from reduced Pdx to P450cam. The natural logarithm of the association constant, Ka, was linearly reduced by the osmotic pressure, and osmotic stress yields uptake of 25 waters on the association. In contrast, uptake of only 13 waters is observed from the osmotic pressure dependence of the association in the non-physiological redox partners, P450cam and oxidized Pdx. Although the general protein-protein associations proceed through the dehydration around the complex interface, the interfacial waters could mediate the hydrogen-bonding interactions. Therefore, about 10 more interfacial waters imply the additional water-mediated hydrogen-bonding network in the P450cam/reduced Pdx complex, which does not exist in the complex with oxidized Pdx. It is also possible that the water-mediated hydrogen-bonding interactions support a high P450cam affinity of reduced (Ka = 0.83 mu M-1) relative to oxidized Pdx (Ka = 5.8 mu M-1). This study points to a novel role of solvents in assisting redox-state-dependent interaction between P450cam and Pdx.


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