Bacillus subtilis cytochromes

The simpler cytochrome bc] complexes of bacteria such as E. coli,102 Paracoccus dentrificans,116 and the photosynthetic Rhodobacter capsulatus117 all appear to function in a manner similar to that of the large mitochondrial complex. The bc] complex of Bacillus subtilis oxidizes reduced menaquinone (Fig. 15-24) rather than ubiquinol.118 In chloroplasts of green plants photochemically reduced plastoquinone is oxidized by a similar complex of cytochrome b, c-type cytochrome /, and a Rieske Fe-S protein.119 120a This cytochrome b6f complex delivers electrons to the copper protein plastocyanin (Fig. 23-18). 

Matsunaga I, Ueda A, Fujiwara N, Sumimoto T, Ichihara K (1999) Characterization of the ybdT gene product of Bacillus subtilis novel fatty acid (3-hydroxylating cytochrome P450. Lipids 34 841-846... 

Lentz, O., Urlacher, V., and Schmid, R. D. 2004 Substrate specificity of native and mutated cytochrome P450 (CYP102A3) from Bacillus subtilis. J. Biotechnol., 108, 41-A9. 

Lawson RJ, von Wachenfeldt C, Haq I, Perkins J, Munro AW. Expression and characterization of the two flavodoxin proteins of Bacillus subtilis, YkuN and YkuP biophysical properties and interactions with cytochrome P450. Biochemistry 2004 43 12390-12409. 

The membrane-bound cytochrome 655s (Bacillus subtilis) contains, according to secondary structure predictions, five transmembrane helices. It functions to anchor two other subunits of the succinate quinone oxidoreductase complex (complex II, E.C. 1.3.5.1) in the cytoplasmic membrane (68). The 1.3-2.0 hemes per covalently bound flavin have been found with the isolated enzyme. The amino acid residues that bind the heme between the a-helices are likely bis(histidine). The EPR and NIR MCD spectra are consistent with this because the EPR spectra show a g value of 3.4 with a HALS lineshape, and the MCD spectra show a low-spin CT band at 1600 nm with Ae of 380 M cm at 4.2 K and 5 T (69). This appears to be another example of a bis(histi-dine)-coordinated heme with near perpendicular alignment of the ligands. 

Lee, D.-S., A. Yamada, H. Sugimoto, I. Matsunaga, H. Ogura, K. Ichihara et al. (2003). Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 from Bacillus subtilis. J. Biol. Chem. 278, 9761-9767. 

G.A. Reid, C. von Wachenfeldt, and S.K. Chapman (2003). Expression, purification and characterisation of a Bacillus subtilis ferredoxin A potential electron transfer donor to cytochrome P450 Biol. J. Inorg. Biochem. 93, 92-99. 

Stok, J.E. and J.J. De Voss (2000). Expression, purification, and characterization of Biol A carbon-carbon bond cleaving cytochrome P450 involved in biotin biosynthesis in Bacillus subtilis. Arch. Biochem. Biophys. 384, 351-360. 

L.G. Quaroni, I.D.G. Macdonald et al. (2001). Expression, purification and characterization of cytochrome P450 Biol A novel P450 involved in biotin synthesis in Bacillus subtilis. J. Biol. Inorg. Chem. 6, 523-533. 

Lee DS, Yamada A, Sugimoto H, Matsunaga 1, Ogura H, Ichihara K, Adachi S, Park SY, Shiro Y (2003) Substrate recognition and molecular mechanism of fatty acid hydroxylation by cytochrome P450 imm Bacillus subtilis. Crystallographie, speetroseopie, and mutational studies. J Biol Chem 278 9761-9767... 

Cryle MJ, Bell SG, Schlichting I (2010) Structural and biochemical characterization of the cytochrome P450 CypX (CYP134A1) from bacillus subtilis a... 

Lawson RJ, Leys D, Sutcliffe MJ, Kemp CA, Cheesman MR, Smith SJ, Clarkson J, Smith WE, Haq I, Perkins JB et al (2004) Thermodynamic and biophysical characterization of cytochrome p450 Biol from Bacillus subtilis. Biochemistry 43 12410-12426... 

Lee DS, Yamada A, Matsunaga I, Ichihara K, Ada-chi S, Park SY, Shiro Y (2002) Crystallization and preliminary X-ray diffraction analysis of fatty-acid hydroxylase cytochrome P450BS beta from Bacillus subtilis. Acta Crystallogr D Biol Crystallogr 58 687-689... 

Shoji O, Fujishiro T, Nagano S, Tanaka S, Hirose T, Shiro Y, Watanabe Y (2010) Understanding substrate misrecognition of hydrogen peroxide dependent cytochrome P450 from Bacillus subtilis. J Biol InorgChem 15 1331-1339... 

Fig. 7.5 Phylogenetic relationship of A-type cytochrome c oxidase and ubiquinol oxidase subunit I. The clades of cytochrome c oxidase subunit I (CtaD or Coxl) are separated from those of ubiquinol oxidase subunit I (CyoB, CyaA, or QoxB). In this figure, the clade of cytochrome c oxidase includes several microbes from yeast, a-Proteobacteria (a), /, y-Proteobacieria (fi. y, and Actinobacteria the clade of ubiquinol oxidase includes several bacteria from Firmicules, a-Proteohacteria (a), j),y-Proteobacteria (P, y), and acetic acid bacteia (AAB). The gene organizations for the Bacillus subtilis eta gene operon, Escherichia coli cyo operon, and cya operon and ctaBjctaD operon of Acetobacter pasteurianus (AAB) are also shown...

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