about
Protein design: toward functional metalloenzymesInner- and outer-sphere metal coordination in blue copper proteinsBackbone dynamics of plastocyanin in both oxidation states. Solution structure of the reduced form and comparison with the oxidized stateCrystal structure of a bacterial endospore coat component. A laccase with enhanced thermostability propertiesMetal-binding loop length and not sequence dictates structureDefining the Role of the Axial Ligand of the Type 1 Copper Site in Amicyanin by Replacement of Methionine with LeucineRationally tuning the reduction potential of a single cupredoxin beyond the natural rangeMetal templated design of protein interfacesType-zero copper proteinsOuter-Sphere Effects on Reduction Potentials of Copper Sites in Proteins: The Curious Case of High Potential Type 2 C112D/M121E Pseudomonas aeruginosa AzurinBilirubin oxidase from Myrothecium verrucaria: X-ray determination of the complete crystal structure and a rational surface modification for enhanced electrocatalytic O2 reductionAzurin as a Protein Scaffold for a Low-coordinate Nonheme Iron Site with a Small-molecule Binding PocketVariations in methanobactin structure influences copper utilization by methane-oxidizing bacteriaElectron Flow through Nitrotyrosinate in Pseudomonas aeruginosa AzurinCopper-sulfenate complex from oxidation of a cavity mutant of Pseudomonas aeruginosa azurin"Anion clamp" allows flexible protein to impose coordination geometry on metal ionsA Crystallographic Examination of Predisposition versus Preorganization in de Novo Designed MetalloproteinsBeyond the passive interactions at the nano-bio interface: evidence of Cu metalloprotein-driven oxidative dissolution of silver nanoparticlesResonant inelastic X-ray scattering on ferrous and ferric bis-imidazole porphyrin and cytochrome c: nature and role of the axial methionine-Fe bondMultiple Osmotic Stress Responses in Acidihalobacter prosperus Result in Tolerance to Chloride Ions.Reversible S-nitrosylation in an engineered azurinA Euclidean Perspective on the Unfolding of Azurin: Spatial Correlations.An NMR view of the unfolding process of rusticyanin: Structural elements that maintain the architecture of a beta-barrel metalloproteinRedox state dependence of axial ligand dynamics in Nitrosomonas europaea cytochrome c552Factors influencing the energetics of electron and proton transfers in proteins. What can be learned from calculations.Role of protein frame and solvent for the redox properties of azurin from Pseudomonas aeruginosa.Low temperature 65Cu NMR spectroscopy of the Cu+ site in azurin.Metal ions as matchmakers for proteins.Fundamental signatures of short- and long-range electron transfer for the blue copper protein azurin at Au/SAM junctionsCalix[6]tren and copper(II): a third generation of funnel complexes on the way to redox calix-zymes.Anatomy of a red copper center: spectroscopic identification and reactivity of the copper centers of Bacillus subtilis Sco and its Cys-to-Ala variants.Elemental economy: microbial strategies for optimizing growth in the face of nutrient limitation.Long-range electron transferCopper binding to the Alzheimer's disease amyloid precursor proteinTransforming a blue copper into a red copper protein: engineering cysteine and homocysteine into the axial position of azurin using site-directed mutagenesis and expressed protein ligation.Electrochemical and homogeneous electron transfers to the Alzheimer amyloid-beta copper complex follow a preorganization mechanism.Laser-flash photolysis indicates that internal electron transfer is triggered by proton uptake by Alcaligenes xylosoxidans copper-dependent nitrite reductase.The catalytic copper of peptidylglycine alpha-hydroxylating monooxygenase also plays a critical structural roleDetermination of the geometric structure of the metal site in a blue copper protein by paramagnetic NMRBasic requirements for a metal-binding site in a protein: the influence of loop shortening on the cupredoxin azurin.
P2860
Q26866201-CF061BCE-73EE-4182-8B09-57D1E6D93333Q26996087-57F5D2F5-906B-4C8B-83C9-03B26351D7DCQ27634152-E56AB1F3-3642-4452-B0EE-DB24919D4E79Q27640698-6E4BEC32-E179-4B7C-B2FB-CA7FE288AFEBQ27654212-7084AA9E-59EC-426F-826C-F45D582F8480Q27657215-1AFB60E9-B546-4CE4-8058-3EB50D2E2F6CQ27658066-22D69421-96EF-47BB-BEE3-279BF4C57E86Q27658986-BB49D3AD-0EF9-4AE6-B5FB-BF75D93AB726Q27660299-531D5021-3D63-45CF-9469-A5AB7F482F17Q27664747-4E72A293-8AD2-4E16-B6A2-405B04FFC8F0Q27667730-E46745E7-6478-4A80-853E-640085EF4CD9Q27675182-0DF04A4F-9A5F-42F6-B00B-77AE1F69F3F8Q27679072-A4A07906-1913-4C30-9960-388C6D787582Q27679107-B8B69CD1-B703-4E19-9BAD-5F255842C81CQ27681190-E2D7146D-C3F8-4EE9-8884-A95511CC8D30Q27700147-94DA4F71-DD76-4F6C-81A3-1878445A78D5Q27727705-7ED4412D-3B37-4371-8041-CC2C76ABF8F6Q28384716-DEACA4BD-CE75-4D1B-A5AF-85A5E9830AC4Q28385799-EA585E2F-174F-4BFC-9DE0-6374BDC1C51DQ28817920-49F1894F-297C-4B57-983D-C7F2F298B102Q28829213-EE91F768-6878-4FE7-9CEF-666B540FDEB3Q30155060-F02BF4E8-3C3B-470F-99FA-13BB02317441Q30160192-20FDE077-4DB3-4119-9BD6-7EBB562E7663Q30352565-03004D81-0C43-4C29-B0A3-C14F27598517Q30356246-048BABA9-AA9D-4070-8C70-0CACBA9D861BQ30358878-CC15CDBC-FC97-4DB2-A040-D4107F8A3A65Q30491880-7863ECC9-5013-41CF-8D54-23F2680F139BQ33719945-13F5814D-FEE9-4C62-A3CA-F1063F3116D3Q33733813-CD562E25-79E3-4EF4-A85A-599ECF2498D6Q33784454-28304893-6A35-4432-9470-461711B4C39CQ33907362-42022F28-D2FF-4808-BA02-4150BB1F8C58Q33911028-78EF46D1-1217-47F0-8FB4-F58CB0E1FE38Q33928458-4AE19B97-FE14-4CB3-9484-AC8DC279A86CQ34063609-E0299CFE-52DE-4DC9-A06D-5F6E0DEF261DQ34089549-A617D434-B45D-427A-B800-799E91F10847Q34182514-080B75FD-FBA5-44FE-BBDC-7565CEF611C4Q34247672-60EB4511-3FF6-4E14-BA6A-E7E1FAC693CBQ34351773-05D873C7-EE4E-4621-95A1-4719B32C727BQ34478524-8053122D-2633-4A27-97F5-340DBF4E19B2Q34624435-E16A507D-79A8-4D08-AA4E-D0AB0F0DC5DF
P2860
description
2000 nî lūn-bûn
@nan
2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հոտեմբերին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Copper coordination in blue proteins.
@ast
Copper coordination in blue proteins.
@en
Copper coordination in blue proteins.
@nl
type
label
Copper coordination in blue proteins.
@ast
Copper coordination in blue proteins.
@en
Copper coordination in blue proteins.
@nl
prefLabel
Copper coordination in blue proteins.
@ast
Copper coordination in blue proteins.
@en
Copper coordination in blue proteins.
@nl
P356
P1476
Copper coordination in blue proteins.
@en
P2093
Malmström BG
Williams RJ
P2888
P304
P356
10.1007/S007750000146
P577
2000-10-01T00:00:00Z