about
Cryptic proteolytic activity of dihydrolipoamide dehydrogenaseSubstrate interactions with human ferrochelataseA pi-helix switch selective for porphyrin deprotonation and product release in human ferrochelatase.Porphyrin Binding and Distortion and Substrate Specificity in the Ferrochelatase Reaction: The Role of Active Site ResiduesProduct Release Rather than Chelation Determines Metal Specificity for FerrochelataseEvolution in a family of chelatases facilitated by the introduction of active site asymmetry and protein oligomerizationCrystal structure of the catalytic subunit of magnesium chelataseIdentification and characterization of an inhibitory metal ion-binding site in ferrochelataseThe structure and function of frataxin.Living with iron (and oxygen): questions and answers about iron homeostasis.Nickel(II) chelatase variants directly evolved from murine ferrochelatase: porphyrin distortion and kinetic mechanism.Metal ion substrate inhibition of ferrochelatase.Resonance Raman Spectroscopic Examination of Ferrochelatase-induced Porphyrin Distortion.FERROCHELATASE: THE CONVERGENCE OF THE PORPHYRIN BIOSYNTHESIS AND IRON TRANSPORT PATHWAYSMolecular insights into frataxin-mediated iron supply for heme biosynthesis in Bacillus subtilisThe Structure of the Complex between Yeast Frataxin and Ferrochelatase: CHARACTERIZATION AND PRE-STEADY STATE REACTION OF FERROUS IRON DELIVERY AND HEME SYNTHESIS.Identification and characterization of solvent-filled channels in human ferrochelatase.Iron-sulfur cluster synthesis, iron homeostasis and oxidative stress in Friedreich ataxia.Advancements in the pathophysiology of Friedreich's Ataxia and new prospects for treatments.Structure and function of enzymes in heme biosynthesis.Direct measurement of metal ion chelation in the active site of human ferrochelatase.Prokaryotic Heme Biosynthesis: Multiple Pathways to a Common Essential Product.Factors controlling the reactivity of divalent metal ions towards pheophytin aStructural basis of the iron storage function of frataxin from single-particle reconstruction of the iron-loaded oligomer.Metal ion selectivity and substrate inhibition in the metal ion chelation catalyzed by human ferrochelatase.Modulation of inhibition of ferrochelatase by N-methylprotoporphyrin.The catalytic power of magnesium chelatase: a benchmark for the AAA(+) ATPases.Formation and dynamic behavior of mono- and bimetallic cadmium(II) porphyrin complexes: allosteric control of coupled intraligand metal migrations.Conformational control of nonplanar free base porphyrins: towards bifunctional catalysts of tunable basicity.Production and characterization of partially purified extracellular thermostable α-amylase by Bacillus subtilis in submerged fermentation (SmF).Metal and redox selectivity of protoporphyrin binding to the heme chaperone CcmE.Ferrochelatase π-helix: Implications from examining the role of the conserved π-helix glutamates in porphyrin metalation and product release.
P2860
Q24684609-2656A867-E10B-41BD-ACAB-E00B704CEA2CQ27643699-9EEF46E5-D733-47CF-A23F-C4BF1F0D05F5Q27648381-23C5D010-277F-482D-91E7-0A35D281215EQ27650397-DBA1AD90-F960-4A19-8CF1-24A36BE010C8Q27657142-33FCE0B3-2A4F-4FAB-BC41-E7C1197FE4B8Q27666360-46760F35-F673-4FAA-8497-15A4A00F891AQ27707960-0595D777-E1C9-4025-8FA3-2B715F6881D4Q30497754-B685403F-891C-401F-A448-9935E01B8841Q33808205-9291DB3B-68A3-4F00-8DB4-E47FED3C3E24Q34055551-D0AFBD83-7B8A-49AC-A95E-531EF68823D4Q34631621-CFD1A33C-39CE-4054-9B38-FD29361A24F1Q34656625-566C9A7A-B098-4DEB-9FC1-362F4CBE5A6BQ35110484-1426B4A9-C039-419F-87A3-446260F257EBQ35165701-4478A977-CA3F-4FD4-9425-92A344A03F45Q35590961-4783A0B0-A555-4DDC-8BF5-0B0068C9B0AFQ35973559-D89A84F6-5801-4EAB-A454-C0256B89B387Q36250117-4E1421CA-7570-4D66-B29A-3ECF73E0797CQ36488119-56B5DB1B-5799-484E-A6AA-1C5ED2EFDB6CQ36863208-9ADAEA14-605C-47A4-9AE9-EFD5ABD3CE2EQ37761084-EC8266D5-A756-453C-807A-D31BD60C6651Q38621097-865483D8-3584-457A-8AA5-5F9AE17A9740Q39103477-09547626-ABEA-43A5-99AC-69F9CCE97C1AQ41062606-CE05B1B1-4604-4990-A669-BE512EC128EFQ41762099-301BFE41-009F-4A98-843D-9B7DC6585138Q42132519-2B4CC8B4-7EBE-4AE9-922E-519CB7D69805Q42156074-32362125-53EC-4733-9B2F-77F44B28C7FBQ42362006-8602EBFC-5290-42B7-877D-F08F0435DA02Q43476256-AD5C52A5-234B-4164-A66E-E7487CC3AB60Q49953607-1B449C20-5D33-4FF8-926D-F0CBEF13AF38Q51003601-9252DD1E-7972-4AD4-BDF9-35F4D8BD2069Q53440173-29B68B01-0B58-457D-8E91-7A010D9B2FA2Q53841200-10A9D90F-646F-495D-B139-50AB5102A9DC
P2860
description
2006 nî lūn-bûn
@nan
2006 թուականի Մարտին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի մարտին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年論文
@yue
2006年論文
@zh-hant
2006年論文
@zh-hk
2006年論文
@zh-mo
2006年論文
@zh-tw
2006年论文
@wuu
name
Chelatases: distort to select?
@ast
Chelatases: distort to select?
@en
Chelatases: distort to select?
@nl
type
label
Chelatases: distort to select?
@ast
Chelatases: distort to select?
@en
Chelatases: distort to select?
@nl
prefLabel
Chelatases: distort to select?
@ast
Chelatases: distort to select?
@en
Chelatases: distort to select?
@nl
P2093
P2860
P3181
P1476
Chelatases: distort to select?
@en
P2093
Gloria C Ferreira
Grazia Isaya
John A Shelnutt
Mats Hansson
P2860
P304
P3181
P356
10.1016/J.TIBS.2006.01.001
P407
P577
2006-02-15T00:00:00Z