Discovery and characterization of heme enzymes from unsequenced bacteria: Application to microbial lignin degradation

Margaret E. Brown, Mark C. Walker, Toshiki G. Nakashige, Anthony T. Iavarone, Michelle C.Y. Chang

Research output: Contribution to journalArticlepeer-review

93 Scopus citations

Abstract

Bacteria and other living organisms offer a potentially unlimited resource for the discovery of new chemical catalysts, but many interesting reaction phenotypes observed at the whole organism level remain difficult to elucidate down to the molecular level. A key challenge in the discovery process is the identification of discrete molecular players involved in complex biological transformations because multiple cryptic genetic components often work in concert to elicit an overall chemical phenotype. We now report a rapid pipeline for the discovery of new enzymes of interest from unsequenced bacterial hosts based on laboratory-scale methods for the de novo assembly of bacterial genome sequences using short reads. We have applied this approach to the biomass-degrading soil bacterium Amycolatopsis sp. 75iv2 ATCC 39116 (formerly Streptomyces setonii and S. griseus 75vi2) to discover and biochemically characterize two new heme proteins comprising the most abundant members of the extracellular oxidative system under lignin-reactive growth conditions.

Original languageEnglish (US)
Pages (from-to)18006-18009
Number of pages4
JournalJournal of the American Chemical Society
Volume133
Issue number45
DOIs
StatePublished - Nov 16 2011
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Catalysis
  • General Chemistry
  • Biochemistry
  • Colloid and Surface Chemistry

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