AN ACID-STABLE CYTOCHROME IN IRON-OXIDIZING LEPTOSPIRILLUM-FERROOXIDANS
UNSPECIFIED (1991) AN ACID-STABLE CYTOCHROME IN IRON-OXIDIZING LEPTOSPIRILLUM-FERROOXIDANS. FEMS MICROBIOLOGY LETTERS, 81 (1). pp. 89-94. ISSN 0378-1097Full text not available from this repository.
A novel, apparently acid-stable cytochrome has been purified from Leptospirillum ferrooxidans in which it probably functions in the 'downhill' transfer of electrons from ferrous iron. It appeared to comprise a single polypeptide of apparent M(r) 17.9 kDa as determined by SDS-PAGE. Non-denaturing PAGE showed this to be the approximate size of the native protein. The oxidized cytochrome showed a broad absorption maximum at 422 nm and was readily reduced with dithionite or ferrous iron to give a form with absorption maxima at 440 and 579 nm. A mid-point potential of +680 mV at pH 3.5 was determined. Iron and zinc were found at concentrations approaching one atom of each per cytochrome molecule.
|Item Type:||Journal Article|
|Subjects:||Q Science > QR Microbiology|
|Journal or Publication Title:||FEMS MICROBIOLOGY LETTERS|
|Publisher:||ELSEVIER SCIENCE BV|
|Date:||1 June 1991|
|Number of Pages:||6|
|Page Range:||pp. 89-94|
Actions (login required)