Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides.
about
Posttranslational biosynthesis of the protein-derived cofactor tryptophan tryptophylquinoneMutagenesis of tryptophan199 suggests that hopping is required for MauG-dependent tryptophan tryptophylquinone biosynthesisDiradical intermediate within the context of tryptophan tryptophylquinone biosynthesisProline 107 Is a Major Determinant in Maintaining the Structure of the Distal Pocket and Reactivity of the High-Spin Heme of MauGHomemade cofactors: self-processing in galactose oxidase.MauG: a di-heme enzyme required for methylamine dehydrogenase maturation.A catalytic di-heme bis-Fe(IV) intermediate, alternative to an Fe(IV)=O porphyrin radical.A Trp199Glu MauG variant reveals a role for Trp199 interactions with pre-methylamine dehydrogenase during tryptophan tryptophylquinone biosynthesisUncovering novel biochemistry in the mechanism of tryptophan tryptophylquinone cofactor biosynthesis.MauG, a diheme enzyme that catalyzes tryptophan tryptophylquinone biosynthesis by remote catalysis.Tryptophan tryptophylquinone biosynthesis: a radical approach to posttranslational modification.Kinetic mechanism for the initial steps in MauG-dependent tryptophan tryptophylquinone biosynthesisA Suicide Mutation Affecting Proton Transfers to High-Valent Hemes Causes Inactivation of MauG during Catalysis.Ascorbate protects the diheme enzyme, MauG, against self-inflicted oxidative damage by an unusual antioxidant mechanism.Properties of the high-spin heme of MauG are altered by binding of preMADH at the protein surface 40 Å away.
P2860
Q24563330-A1D1E3D1-26A6-45CE-B480-1D3BCDDA99E2Q27674714-B55038C6-1C77-4E15-9108-BE97050F0FDAQ27676809-7DED0863-7366-49D6-A769-0A2BDB4C8BB4Q27677014-A0495AA7-5B23-4450-B9C1-0722E9051234Q33948866-9CEB8C07-ED79-4267-BCA5-A2FAC9D0F1FBQ36592463-1B27724E-D533-4467-9A6A-5F123DED93C3Q36735315-F9BBE07D-492E-45A9-8662-D2C0E6841BCFQ37104425-75DB86F2-C77B-49A0-AD3C-04F89E60E126Q37359679-7E10F00D-E883-4588-9C09-DF6E44B5518AQ37624564-80F4C27D-4551-463B-90E4-D3D2D8E90510Q37982234-B0AD6158-CFE6-4BA6-B9EF-7E4AB8D3647AQ41822500-5D362931-3075-4A2D-838F-6408E74CC8CBQ41990838-71DC0C98-C209-4DA9-B151-4187C415CA43Q46347082-832AEE4A-D2A4-40A0-B6FD-0D18F9BFCFA6Q48170764-C61900B8-0361-4B48-A4EA-D8E58D73B348
P2860
Heterologous expression of correctly assembled methylamine dehydrogenase in Rhodobacter sphaeroides.
description
1999 nî lūn-bûn
@nan
1999年の論文
@ja
1999年学术文章
@wuu
1999年学术文章
@zh-cn
1999年学术文章
@zh-hans
1999年学术文章
@zh-my
1999年学术文章
@zh-sg
1999年學術文章
@yue
1999年學術文章
@zh
1999年學術文章
@zh-hant
name
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@en
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@nl
type
label
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@en
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@nl
prefLabel
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@en
Heterologous expression of cor ...... se in Rhodobacter sphaeroides.
@nl
P2093
P2860
P1476
Heterologous expression of cor ...... ase in Rhodobacter sphaeroides
@en
P2093
B V Sharma
J P Hosler
M E Graichen
R J van Spanning
V L Davidson
P2860
P304
P407
P577
1999-07-01T00:00:00Z