Ferredoxin-linked chloreplast enzymes. Progress report, August 15, 1990--August 14, 1993

Technical Report · Mon Jan 01 04:00:00 EST 1996

DOI:https://doi.org/10.2172/167156· OSTI ID:167156

Progress has clearly been made on all of the goals set forth in the original proposal. Although the monoclonal antibodies raised against FNR turned out no to be useful for mapping the FNR/ferredoxin or FNR/NADP+ interaction domains, good progress has been made on mapping the FNR/ferredoxin interaction domains by an alternative technique, differential chemical modification. Furthermore, the techniques developed for differential chemical modifications of these two proteins - taurine modification of aspartate and glutamate residues and biotin modification of lysine residues - should be useful for mapping the interaction domains of many proteins that associate through electrostatic interactions. Finally, progress has also been made with respect to another ferredoxin-dependent enzyme involved in the earliest steps of plant nitrogen metabolism - nitrite reductase. Questions concerning the subunit composition and heme content of the enzyme have been resolved and evidence demonstrating the involvement of lysine and arginine residues in binding ferredoxin has been obtained for the first time.

• Research Organization: Texas Tech Univ., Lubbock, TX (United States)
• Sponsoring Organization: USDOE, Washington, DC (United States)
• DOE Contract Number: FG05-90ER20017
• OSTI ID: 167156
• Report Number(s): DOE/ER/20017--T1; ON: DE96003867
• Country of Publication: United States
• Language: English

Related Subjects

55 BIOLOGY AND MEDICINE
BASIC STUDIES
AMINO ACID SEQUENCE
ARGININE
BIOCHEMICAL REACTION KINETICS
BIOTIN
CHLOROPLASTS
ENZYMES
FERREDOXIN
LYSINE
MAPPING
METABOLISM
MONOCLONAL ANTIBODIES
PROGRESS REPORT
SPINACH
TAURINE