Abstract
Summary An iron-sulfur protein containing eight iron atoms and eight acid-labile sulfur atoms per one molecule of 19,000 daltons was found in Pseudomonas ovalis which had been grown on medium supplemented with glucose and ammonium sulfate. This protein molecule was composed of two subunits of identical size. The absorption spectrum exhibited a peak at 283 nm with shoulders at 320 nm and 400 nm. The purified iron-sulfur protein catalyzed the photorenduction of NAFP by spinach chloroplast.
Sign-in/Register to access full text options 
Talk to us
Join us for a 30 min session where you can share your feedback and ask us any queries you have
Schedule a callMore From: Biochemical and Biophysical Research Communications
Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.
