| Literature DB >> 17816020 |
C A Appleby, J D Tjepkema, M J Trinick.
Abstract
A dimeric hemoglobin was purified from nitrogen-fixing root nodules formed by association of Rhizobium with a nonleguminous plant, Parasponia. The oxygen dissociation rate constant is probably sufficiently high to allow Parasponia hemoglobin to function in a fashion similar to that of leghemoglobin, by oxygen buffering and transport during symbiotic nitrogen fixation. The identification of hemoglobin in a nonlegume raises important questions about the evolution of plant hemoglobin genes.Entities:
Year: 1983 PMID: 17816020 DOI: 10.1126/science.220.4600.951
Source DB: PubMed Journal: Science ISSN: 0036-8075 Impact factor: 47.728