Abstract
Bacterial HCN production is catalyzed by the membrane-bound enzyme HCN synthase. HCN synthase is encoded by a cluster of three genes, hcnABC, which form an operon. Polymorphism in the three genes may affect the catalytic efficiency of the enzyme and influence HCN production. In this study, we selected a ∼570 bp portion of hcnAB gene consisting of a cysteine cluster at the 3′ end of hcnA that matches the iron-sulfur binding signature of 2[Fe–S] ferredoxins and the ADP binding-fold in the 5′ end of hcnB from 50 strains of HCN producing bacteria to analyze polymorphism in the gene. Both motifs have been credited to have a role in bacterial HCN synthesis. Analysis of the partial hcnAB gene showed that the bacteria grouped into four groups. Pairwise comparison of the distinctness ratios revealed that the HCN groups identified in this study were ecologically distinct populations and distinctness between the groups was reflected in HCN production by the bacteria. Supplementary materials are available for this article. Go to the publisher's online edition of Geomicrobiology Journal to view the supplemental file.
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 callDisclaimer: 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.
