title: [Oligomeric state investigation of flavocytochrome CYP102A1 using AFM with standard and supersharp probes].
abstract: Atomic force microscopy with two types of probes - standard (radius of curvature R approximately 10 nm) and supersharp (R approximately 2 nm)- was used to determine CYP102A1oligomeric state. CYP102A1 images were obtained in a liquid, air and vacuum environment using the standard probes, also a ratio of monomers to oligomers (alpha) of CYP102A1 were determined as alpha=0.48:0.52. At the same time use of standard probes did not allow to resolve the structure of these oligomers. Supersharp probes allowed to obtain the data about the monomers to oligomers ratio, and also about the dimers/trimers/tetramers ratio in air and vacuum. So, a ratio alpha of CYP102A1 in liquid can be determined by the standard probes, and an oligomeric state of protein can be specified by the supersharp probes.
authors: Iu D
authors: IuD
authors: Ivanov
authors: N S
authors: NS
authors: Bukharina
authors: P A
authors: PA
authors: Frantsuzov
authors: N V
authors: NV
authors: Krokhin
authors: S L
authors: SL
authors: Kanashenko
authors: A I
authors: AI
authors: Archakov
mesh_terms: D001426:Bacterial Proteins / Q000737:chemistry*; D003577:Cytochrome P-450 Enzyme System / Q000737:chemistry*; D018625:Microscopy, Atomic Force; D009097:Multienzyme Complexes / Q000737:chemistry* / Q000648:ultrastructure*; D009251:NADPH-Ferrihemoprotein Reductase / Q000737:chemistry*; D020836:Protein Structure, Quaternary
chemical_list: D001426:Bacterial Proteins; D009097:Multienzyme Complexes; D003577:Cytochrome P-450 Enzyme System; D009251:NADPH-Ferrihemoprotein Reductase; C052423:flavocytochrome P450 BM3 monoxygenases