Characterization of 3-Ketosteroid 9α-Hydroxylase, a Rieske Oxygenase in the Cholesterol Degradation Pathway ofMycobacterium tuberculosis

Characterization of a Second Rhodococcus erythropolis SQ1 3-Ketosteroid 9 -Hydroxylase Activity Comprising a Terminal Oxygenase Homologue, KshA2, Active with Oxygenase-Reductase Component KshB

(2008) R. van der Geize et al.   APPLIED AND ENVIRONMENTAL MICROBIOLOGY

3-Keto-5α-steroid Δ1-dehydrogenase fromRhodococcus erythropolisSQ1 and its orthologue inMycobacterium tuberculosisH37Rv are highly specific enzymes that function in cholesterol catabolism

(2008) Jan Knol et al.   BIOCHEMICAL JOURNAL

Searching protein structure databases with DaliLite v.3

(2008) L. Holm et al.   BIOINFORMATICS

Non-heme iron-dependent dioxygenases: unravelling catalytic mechanisms for complex enzymatic oxidations

(2008) Timothy DH Bugg et al.   CURRENT OPINION IN CHEMICAL BIOLOGY

Tuberculous Granulomas Are Hypoxic in Guinea Pigs, Rabbits, and Nonhuman Primates

(2008) L. E. Via et al.   INFECTION AND IMMUNITY

Versatility of biological non-heme Fe(II) centers in oxygen activation reactions

(2008) Elena G Kovaleva et al.   Nature Chemical Biology

Mycobacterial persistence requires the utilization of host cholesterol

(2008) A. K. Pandey et al.   PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA