The cytochromes ofEscherichia coli

Culture optimization ofEscherichia coli for expression ofgE proteinfrombovine herpesvirus 1 and 5

Background The use of Escherichia coli for the production of recombinant proteins is an established strategy to obtain biotechnological tools. However, the recombinant protein expression is dependent on temperature, bacterial culture time, induction period, nutrients, plasmid characteristics, and insert itself. Thus, the aim of this study was optimize the expression of recombinant gE protein (r...

Hydroxylation of testosterone by bacterial cytochromes P450 using the Escherichia coli expression system.

Two hundred thirteen cytochrome P450 (P450) genes were collected from bacteria and expressed based on an Escherichia coli expression system to test their hydroxylation ability to testosterone. Twenty-four P450s stereoselectively monohydroxylated testosterone at the 2alpha-, 2beta-, 6beta-, 7beta-, 11beta-, 12beta-, 15beta-, 16alpha-, and 17-positions (17-hydroxylation yields 17-ketoproduct). Th...

Potentiometric analysis of the cytochromes of an Escherichia coli mutant strain lacking the cytochrome d terminal oxidase complex.

A combination of potentiometric analysis and electrochemically poised low-temperature difference spectroscopy was used to examine a mutant strain of Escherichia coli that was previously shown by immunological criteria to be lacking the cytochrome d terminal oxidase. It was shown that this strain is missing cytochromes d, a1, and b558 and that the cytochrome composition of the mutant is similar ...

Cytochromes of aquatic fungi.

The cytochrome systems of two classes of aquatic fungi, the Oomycetes and Chytridiomycetes, were studied by means of reduced-minus-oxidized difference spectra at room and at low temperature. At room temperature, all of these fungi have a c-type cytochrome with an absorption maximum at 551 mmu and a b-type cytochrome at 564 mmu. The Oomycetes have a-type cytochromes at 605 mmu, and the Chytridio...

Repetitions in the polypeptide sequence of cytochromes.