Open AccessNickel uptake and utilization by microorganisms
Author(s) -
Mulrooney Scott B.,
Hausinger Robert P.
Publication year - 2003
Publication title -
fems microbiology reviews
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.91
H-Index - 212
eISSN - 1574-6976
pISSN - 0168-6445
DOI - 10.1016/s0168-6445(03)00042-1
Subject(s) - carbon monoxide dehydrogenase , nickel , biochemistry , enzyme , hydrogenase , permease , microorganism , urease , cofactor , biology , reductase , bacteria , chemistry , carbon monoxide , organic chemistry , transporter , catalysis , genetics , gene
Abstract Nickel is an essential nutrient for selected microorganisms where it participates in a variety of cellular processes. Many microbes are capable of sensing cellular nickel ion concentrations and taking up this nutrient via nickel‐specific permeases or ATP‐binding cassette‐type transport systems. The metal ion is specifically incorporated into nickel‐dependent enzymes, often via complex assembly processes requiring accessory proteins and additional non‐protein components, in some cases accompanied by nucleotide triphosphate hydrolysis. To date, nine nickel‐containing enzymes are known: urease, NiFe–hydrogenase, carbon monoxide dehydrogenase, acetyl–CoA decarbonylase/synthase, methyl coenzyme M reductase, certain superoxide dismutases, some glyoxylases, aci‐reductone dioxygenase, and methylenediurease. Seven of these enzymes have been structurally characterized, revealing distinct metallocenter environments in each case.