about
Isolation, sequencing, and mutagenesis of the gene encoding NAD- and glutathione-dependent formaldehyde dehydrogenase (GD-FALDH) from Paracoccus denitrificans, in which GD-FALDH is essential for methylotrophic growthS-formylglutathione hydrolase of Paracoccus denitrificans is homologous to human esterase D: a universal pathway for formaldehyde detoxification?Two-component system that regulates methanol and formaldehyde oxidation in Paracoccus denitrificansThe organisation of proton motive and non-proton motive redox loops in prokaryotic respiratory systems.Expression of the mau genes involved in methylamine metabolism in Paracoccus denitrificans is under control of a LysR-type transcriptional activator.The cytochrome bd-type quinol oxidase is important for survival of Mycobacterium smegmatis under peroxide and antibiotic-induced stress.Regulation of nitrogen metabolism in the nitrate-ammonifying soil bacterium Bacillus vireti and evidence for its ability to grow using N2 O as electron acceptor.Cytochromes c(550), c(552), and c(1) in the electron transport network of Paracoccus denitrificans: redundant or subtly different in function?Nitrite reductase of Nitrosomonas europaea is not essential for production of gaseous nitrogen oxides and confers tolerance to nitriteIntegration of heterologous DNA into the genome of Paracoccus denitrificans is mediated by a family of IS1248-related elements and a second type of integrative recombination event.Isolation and characterization of the moxJ, moxG, moxI, and moxR genes of Paracoccus denitrificans: inactivation of moxJ, moxG, and moxR and the resultant effect on methylotrophic growthA method for introduction of unmarked mutations in the genome of Paracoccus denitrificans: construction of strains with multiple mutations in the genes encoding periplasmic cytochromes c550, c551i, and c553i.A mutant of Paracoccus denitrificans with disrupted genes coding for cytochrome c550 and pseudoazurin establishes these two proteins as the in vivo electron donors to cytochrome cd1 nitrite reductaseNitrosomonas europaea expresses a nitric oxide reductase during nitrification.Expression of nitrous oxide reductase in Paracoccus denitrificans is regulated by oxygen and nitric oxide through FnrP and NNR.The Low Biomass Yields of the Acetic Acid Bacterium Acetobacter pasteurianus Are Due to a Low Stoichiometry of Respiration-Coupled Proton Translocation.Novel nirK cluster genes in Nitrosomonas europaea are required for NirK-dependent tolerance to nitrite.Isolation and characterization of a novel insertion sequence element, IS1248, in Paracoccus denitrificans.Fine-tuned regulation by oxygen and nitric oxide of the activity of a semi-synthetic FNR-dependent promoter and expression of denitrification enzymes in Paracoccus denitrificans.Nitric oxide oscillations in Paracoccus denitrificans: the effects of environmental factors and of segregating nitrite reductase and nitric oxide reductase into separate cells.Comparison of landfarming amendments to improve bioremediation of petroleum hydrocarbons in Niger Delta soils.The nitrate-ammonifying and nosZ-carrying bacterium Bacillus vireti is a potent source and sink for nitric and nitrous oxide under high nitrate conditions.NosX function connects to nitrous oxide (N2O) reduction by affecting the Cu(Z) center of NosZ and its activity in vivo.Transcription regulation of the nir gene cluster encoding nitrite reductase of Paracoccus denitrificans involves NNR and NirI, a novel type of membrane protein.MauE and MauD proteins are essential in methylamine metabolism of Paracoccus denitrificans.Structural and functional analysis of aa3-type and cbb3-type cytochrome c oxidases of Paracoccus denitrificans reveals significant differences in proton-pump design.Isolation, sequencing and mutational analysis of a gene cluster involved in nitrite reduction in Paracoccus denitrificans.Expression of nitrite reductase in Nitrosomonas europaea involves NsrR, a novel nitrite-sensitive transcription repressor.The oxidation product of molybdenum cofactor from milk xanthine oxidase.Denitrification and ammonia oxidation by Nitrosomonas europaea wild-type, and NirK- and NorB-deficient mutants.Imaging linear and circular polarization features in leaves with complete Mueller matrix polarimetry.Unraveling an FNR based regulatory circuit in Paracoccus denitrificans using a proteomics-based approach.MLPA diagnostics of complex microbial communities: relative quantification of bacterial species in oral biofilms.Expression of the mau gene cluster of Paracoccus denitrificans is controlled by MauR and a second transcription regulator.A benzene-degrading nitrate-reducing microbial consortium displays aerobic and anaerobic benzene degradation pathways.Regulation of expression of terminal oxidases inParacoccus denitrificansThe reduction state of the Q-pool regulates the electron flux through the branched respiratory network of Paracoccus denitrificansFnrP and NNR of Paracoccus denitrificans are both members of the FNR family of transcriptional activators but have distinct roles in respiratory adaptation in response to oxygen limitationNitrite and nitric oxide reduction in Paracoccus denitrificans is under the control of NNR, a regulatory protein that belongs to the FNR family of transcriptional activatorsMicrobial Communities in Sediments From Four Mildly Acidic Ephemeral Salt Lakes in the Yilgarn Craton (Australia) - Terrestrial Analogs to Ancient Mars
P50
Q24675562-7B54829D-A5A8-4FCA-BCB1-59B65590074EQ24681537-88D6AC74-107D-4252-998B-96F73D901A2BQ28492909-5F0E5A1E-CD3A-4DBF-BF02-86872B80CF21Q33377757-85B910F2-3E7F-4F9B-A055-20AFAA41BA69Q34325353-4521260D-A7F3-4C65-B445-3A335D2EDDDDQ35670401-60A810BD-DA97-4B0F-B06E-C5D400EABCE7Q35835352-FD253A42-3775-4751-8311-DEA010BE4A42Q38469888-AB05A8AC-7930-4674-8EA9-542754B48AE7Q39678935-5856E02E-46CB-4B39-95F6-27A691FE57D2Q39838016-0C4BB2DC-8D5D-4686-BB17-BB25A063D860Q39945736-FBD9FCFF-CC8E-4A7B-AD21-C2A4E56FB323Q39945741-F558B934-179B-4701-A201-F82626BE05DCQ39981856-E4BBFF49-96D1-4207-961E-18A649814982Q40909391-69A082F8-AC5A-4415-96E3-9EBE1728891EQ41981633-5C8228ED-513C-4125-9CFA-8FC00AFB5CCEQ42124434-1D5838A8-5F97-4B96-AFD8-76F375905873Q42565110-963D924C-6BB6-4D41-A917-F43BC2B99080Q42672312-6E23CBB1-0641-4441-9A89-89E734124DA9Q44685076-4213E5E3-1AE5-4E8D-8528-23AD6BDBF509Q45019833-9B7AFC80-84AF-465C-8E90-81CB7E3C5A24Q46268074-C05D7326-C9F4-421A-B299-A9E6A3A7CB46Q46323527-B09E0E92-3A14-4C61-92A8-20F5485B96E0Q47750712-F8ADADA3-FA0B-4D4A-A56D-450CAD06A0F1Q47902409-36B2B6DB-9DE3-4BCF-8A52-AD7820B875E7Q48041570-AC7A4A23-7191-4878-BBF4-A452C20E0379Q48063491-91664F22-761F-4C59-AA10-59A3E12A042FQ48086848-408CACD4-3DD1-40A1-8081-E93303BA0FE8Q48838512-33E92B10-0798-4E5E-878D-6B476685CCA8Q50902198-30AFC56B-ED01-43DB-9273-D61676820DF0Q51571064-4FE5BD8C-2B3F-48F0-B012-647DA57C5B1EQ52727334-A490084F-3774-488B-A66C-4F1B265C26F8Q52905853-5B3A695E-963B-4229-9565-DED2502B8A85Q54513959-9AC45224-F873-40EB-89A7-833ECDDC6614Q54570032-100901DA-157D-4DC6-A4FA-303722DD08B4Q55287593-02E9082D-3C3F-4BDB-8FF9-D71783BFB5FCQ57393878-13E4668A-1213-43AB-AC58-D669BBEC8D00Q57393900-4F114DD8-6BC5-46E1-9FDE-C76DB28EA590Q57393915-3075C505-4C95-4B08-A46F-97CDF569C922Q57393938-D4E803B3-254B-46EF-B6CD-A32D1FD21436Q64247279-55118962-FD2A-4BF1-A777-8EB2DD6779E8
P50
description
Forscher
@de
chercheur
@fr
investigador
@es
researcher
@en
ricercatore
@it
wetenschapper
@nl
研究者
@zh
name
R J Van Spanning
@ast
R J Van Spanning
@en
R J Van Spanning
@es
R J Van Spanning
@nl
type
label
R J Van Spanning
@ast
R J Van Spanning
@en
R J Van Spanning
@es
R J Van Spanning
@nl
prefLabel
R J Van Spanning
@ast
R J Van Spanning
@en
R J Van Spanning
@es
R J Van Spanning
@nl
P31
P496
0000-0002-6879-4770