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Langmuir-Blodgett films of cytochrome P450scc were prepared on the solid supports and their spectral properties were investigated. Being immobilized, hemoprotein changes its spin state from initially high to low spin. This transition is reversible since after the solubilization of hemoprotein, the spin state equilibrium is shifted towards high-spin state. Anaerobic reduction of film incorporated cytochrome P450scc by electron transfer chain (NADPH-->adrenodoxin reductase-->adrenodoxin) revealed the low rate of the reaction that coincides well with the content of the hemoprotein low-spin form. We suggest that particularly regular orientation of solid cytochrome P450scc are of crucial importance for this phenomenon.
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