Article citationsMore>>

S. Petkun, R. Shi, Y. Li, A. Asinas, C. Munger, L. Zhang, M. Waclawek, B. Soboh, G. Sawers and M. Cygler, “Structure of Hydrogenase Maturation Protein HypF Reaction Intermediates Shows Two Active Sites,” Structure, Vol. 19, No. 12, 2011, pp. 1773-1783. doi:10.1016/j.str.2011.09.023

has been cited by the following article:

• TITLE: Genomic Analysis of Anabaena variabilis Mutants PK17 and PK84 That Are Characterised by High Production of Molecular Hydrogen

  AUTHORS: Sergey V. Shestakov, Lidia E. Mikheeva, Andrey V. Mardanov, Nikolai V. Ravin, Konstantin G. Skryabin

  KEYWORDS: Cyanobacteria; Hydrogen Metabolism; Hydrogenases; Pyrosequencing; Mutants; Anabaena

  JOURNAL NAME: Advances in Microbiology, Vol.3 No.4, August 6, 2013

  ABSTRACT: The use of cyanobacteria for producing molecular hydrogen is one of the desirable tasks of photobiotechnology. Some years ago, we isolated several chemically induced mutants of the cyanobacterium Anabaena variabilis ATCC 29413 that exhibited a high level of H2-production; but the genetic nature of these mutants remained unresolved. To reveal mutations that could be responsible for enhancement of H2-production in two independent mutants, PK17 and PK84, the pyrosequencing of their entire genomes was performed. The results were analyzed on the basis of comparison with the complete genome sequence of the reference strain Anabaena variabilis ATCC 29413. The genomes of mutants PK17 and RK84 contain 107 and 104 point deviations from the reference genome, respectively. The most probable reason for the increase of H2-production in mutant PK17 is the mutation identified in the gene hupL encoding the large subunit of uptake hydrogenase. A high level of H2-production in mutant PK84 could be the result of a mutation in a conserved part of the gene hypF, which participates in the post-translation maturation of hydrogenase complexes.