Nickel utilization by microorganisms.

Hausinger, Robert P.

doi:10.1128/mmbr.51.1.22-42.1987

Cited by 160 publications

(63 citation statements)

References 136 publications

(197 reference statements)

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“…Nickel is an element essential for the activities of most hydrogenases as well as for urease, methylcoenzyme M reductase and carbon monoxide dehydrogenase in microorganisms [10,11]. Besides nickel, hydrogenase also contains iron-sulphur centers involved in the transfer of electrons in the oxidation of hydrogen or reduction of protons.…”

Section: Introductionmentioning

confidence: 99%

Microbial hydrogenases: Primary structure, classification, signatures and phylogeny

Mandrand

1993

FEMS Microbiology Letters

191

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Thirty sequenced microbial hydrogenases are classified into six classes according to sequence homologies, metal content and physiological function. The first class contains nine H2‐uptake membrane‐bound NiFe‐hydrogenases from eight aerobic, facultative anaerobic and anaerobic bacteria. The second comprises four periplasmic and two membrane‐bound H2 ‐uptake NiFe(Se)‐hydrogenases from sulphate‐reducing bacteria. The third consists of four periplasmic Fe‐hydrogenases from strict anaerobic bacteria. The fourth contains eight methyl‐viologen‐ (MV), factor F420‐ (F420) or NAD‐reducing soluble hydrogenases from methanobacteria and Alcaligenes eutrophus H16. The fifth is the H2‐producing labile hydrogenase isoenzyme 3 of Escherichia coli. The sixth class contains two soluble tritium‐exchange hydrogenases of cyanobacteria. The results of sequence comparison reveal that the 30 hydrogenases have evolved from at least three different ancestors. While those of class I, II, IV and V hydrogenases are homologous, i.e. sharing the same evolutionary origin, both class III and VI hydrogenases are neither related to each other nor to the other classes. Sequence comparison scores, hierarchical cluster structures and phylogenetic trees show that class II falls into two distinct clusters composed of NiFe‐ and NiFeSe‐hydrogenases, respectively. These results also reveal that class IV comprises three distinct clusters: MV‐reducing, F420‐reducing and NAD‐reducing hydrogenases. Specific signatures of the six classes of hydrogenases as well as some subclusters have been detected. Analyses of motif compositions indicate that all hydrogenases, except those of class VI, must contain some common motifs probably participating in the formation of hydrogen activation domains and electron transfer domains. The regions of hydrogen activation domains are highly conserved and can be divided into two categories. One corresponds to the ‘nickel active center’ of NiFe(Se)‐hydrogenases. It consists of two possible specific nickel‐binding motifs, RxCGxCxxxH and DPCxxCxxH, located at the N‐ and C‐termini of so‐called large subunits in the dimeric hydrogenases, respectively. The other is the H‐cluster of the Fe‐hydrogenases. It might comprise three motifs on the C‐terminal half of the large subunits. However, the motifs corresponding to the putative electron transfer domains, as well as their polypeptides chains, are poorly or even not at all conserved. They are present essentially on the small subunits in NiFe‐hydrogenases. Some of these motifs resemble the typical ferredoxin‐like Fe‐S cluster binding site. The variation of the sequences in these regions might determine the specific interaction between the external electron transfer domains of hydrogenases and their electron carriers. For example, the C‐terminal cysteine‐histidine rich region of the small subunits are distinguishable between those of H2‐uptake, H2‐producing, MV‐reducing, F420‐reducing and NAD‐reducing NiFe(Se)‐hydrogenases.

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Section: Introductionmentioning

confidence: 99%

Microbial hydrogenases: Primary structure, classification, signatures and phylogeny

Mandrand

1993

FEMS Microbiology Letters

191

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“…Urease is produced by many species of bacteria, fungi, and plants and is involved in the utilization of urea as a nitrogen source [1]. Urease catalyses the hydrolysis of urea to ammonia and carbonic acid.…”

Section: Introductionmentioning

confidence: 99%

Regulation of urease activity in Rhizobium meliloti

Miksch

1994

FEMS Microbiology Letters

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Using an ureC-lacZ fusion, the expression of urease structural genes of the soil bacterium Rhizobium meliloti strain AK631 was studied in response to different nitrogen sources and nickel contents in the growth medium. The expression of urease genes is repressed by ammonia and is not inducible by urea. Urease activity depends on the nickel concentration of the medium. Nickel uptake is repressed in medium containing ammonia and is not affected by the genes located in the urease operon investigated.

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“…Dot-blot DNA hybridization analysis revealed that the urease gene cluster of K. pneumoniae possesses no significant homology with those of Proteus species and Morganella morganii. [1]. The enzyme cleaves urea into ammonia and carbonic acid, and thus induces a significant increase in the pH of the immediate environment of urease-producing organisms [1].…”

Section: Discussionmentioning

confidence: 99%

“…[1]. The enzyme cleaves urea into ammonia and carbonic acid, and thus induces a significant increase in the pH of the immediate environment of urease-producing organisms [1]. Following colonization of the kidney by urease-producing organisms, such a change in pH has been suggested to induce the formation of kidney stones [21.…”

Section: Discussionmentioning

confidence: 99%