X-ray structure of a blue-copper nitrite reductase in two crystal forms. The nature of the copper sites, mode of substrate binding and recognition by redox partner 1 1Edited by R. Huber

1998 ◽  
Vol 282 (2) ◽  
pp. 369-382 ◽  
Author(s):  
Fraser E Dodd ◽  
Jos Van Beeumen ◽  
Robert R Eady ◽  
S.Samar Hasnain
Keyword(s):  
Nitrite Reductase ◽  
Substrate Binding ◽  
Blue Copper ◽  
Crystal Forms ◽  
X Ray ◽  
Redox Partner ◽  
Copper Sites

X-ray structure of a blue copper nitrite reductase at high pH and in copper-free form at 1.9 Å resolution

2001 ◽  
Vol 57 (8) ◽  
pp. 1110-1118 ◽  
Author(s):  
Mark J. Ellis ◽  
Fraser E. Dodd ◽  
Richard W. Strange ◽  
Miguel Prudêncio ◽  
Gary Sawers ◽  
...  
Keyword(s):  
Nitrite Reductase ◽  
Free Form ◽  
Blue Copper ◽  
X Ray ◽  
High Ph

Insights into Redox Partner Interactions and Substrate Binding in Nitrite Reductase fromAlcaligenes xylosoxidans: Crystal Structures of the Trp138His and His313Gln Mutants†,‡

Biochemistry ◽  
2004 ◽  
Vol 43 (51) ◽  
pp. 16311-16319 ◽  
Author(s):  
Mark L. Barrett ◽  
Roger L. Harris ◽  
Svetlana Antonyuk ◽  
Michael A. Hough ◽  
Mark J. Ellis ◽  
...  
Keyword(s):  
Crystal Structures ◽  
Nitrite Reductase ◽  
Substrate Binding ◽  
Redox Partner

Electronic structure of perturbed blue copper sites: Sulfur K-edge and MCD of stellacyanin and nitrite reductase

1995 ◽  
Vol 59 (2-3) ◽  
pp. 700
Author(s):  
Louis B. LaCroix ◽  
Susan E. Shadle ◽  
Yaning Wang ◽  
Bruce A. Averill ◽  
Britt Hedman ◽  
...  
Keyword(s):  
Electronic Structure ◽  
Nitrite Reductase ◽  
Blue Copper ◽  
Copper Sites

Copper–oxygen Dynamics in Tyrosinase

2019 ◽  
Author(s):  
Nobutaka Fujieda ◽  
Sachiko Yanagisawa ◽  
Minoru Kubo ◽  
Genji Kurisu ◽  
Shinobu Itoh
Keyword(s):  
Catalytic Mechanism ◽  
Substrate Binding ◽  
Active Form ◽  
Copper Ion ◽  
Atomic Resolution ◽  
Oxygen Species ◽  
X Ray ◽  
Oxygen Dynamics ◽  
Insight Into ◽  
Copper Centre

To unveil the activation of dioxygen on the copper centre (Cu<sub>2</sub>O<sub>2</sub>core) of tyrosinase, we performed X-ray crystallograpy with active-form tyrosinase at near atomic resolution. This study provided a novel insight into the catalytic mechanism of the tyrosinase, including the rearrangement of copper-oxygen species as well as the intramolecular migration of copper ion induced by substrate-binding.<br>

Crystal Forms of Semisynthetic Ergot Alkaloid Terguride

2002 ◽  
Vol 67 (4) ◽  
pp. 479-489 ◽  
Author(s):  
Michal Hušák ◽  
Bohumil Kratochvíl ◽  
Ivana Císařová ◽  
Ladislav Cvak ◽  
Alexandr Jegorov ◽  
...  
Keyword(s):  
Crystal Structure ◽  
Ergot Alkaloid ◽  
Simplified Model ◽  
Quantum Mechanical ◽  
Quantum Mechanical Calculations ◽  
X Ray Diffraction ◽  
Torsion Angles ◽  
Crystal Forms ◽  
X Ray ◽  
Independent Molecules

Two new structures of semisynthetic ergot alkaloid terguride created by unusual number of symmetry-independent molecules were determined by X-ray diffraction methods at 150 K. Form A (monoclinic, P212121, Z = 12) contains three symmetry-independent terguride molecules and two molecules of water in the asymmetric part of the unit cell. The form CA (monoclinic, P21, Z = 8) is an anhydrate remarkable by the presence of four symmetry-independent molecules in the crystal structure. Conformations of twelve symmetry-independent molecules that were found in four already described terguride structures are compared with torsion angles obtained by ab initio quantum-mechanical calculations for the simplified model of N-cyclohexyl-N'-diethylurea.

scholarly journals Monitoring protein precipitates by in-house X-ray powder diffraction

2013 ◽  
Vol 28 (S2) ◽  
pp. S458-S469 ◽  
Author(s):  
Kenny Ståhl ◽  
Christian G. Frankær ◽  
Jakob Petersen ◽  
Pernille Harris
Keyword(s):  
Powder Diffraction ◽  
Protein Crystal ◽  
Data Sets ◽  
Crystal Forms ◽  
X Ray ◽  
Cell Parameters ◽  
X Ray Scattering ◽  
Source Organism ◽  
Peak Asymmetry ◽  
Overlapping Peaks

Powder diffraction from protein powders using in-house diffractometers is an effective tool for identification and monitoring of protein crystal forms and artifacts. As an alternative to conventional powder diffractometers a single crystal diffractometer equipped with an X-ray micro-source can be used to collect powder patterns from 1 µl samples. Using a small-angle X-ray scattering (SAXS) camera it is possible to collect data within minutes. A streamlined program has been developed for the calculation of powder patterns from pdb-coordinates, and includes correction for bulk-solvent. A number of such calculated powder patterns from insulin and lysozyme have been included in the powder diffraction database and successfully used for search-match identification. However, the fit could be much improved if peak asymmetry and multiple bulk-solvent corrections were included. When including a large number of protein data sets in the database some problems can be foreseen due to the large number of overlapping peaks in the low-angle region, and small differences in unit cell parameters between pdb-data and powder data. It is suggested that protein entries are supplied with more searchable keywords as protein name, protein type, molecular weight, source organism etc. in order to limit possible hits.

scholarly journals Towards a unified understanding of the copper sites in particulate methane monooxygenase: An X-ray absorption spectroscopic investigation

2021 ◽  
Author(s):  
George Cutsail III ◽  
Matthew O Ross ◽  
Amy C Rosenzweig ◽  
Serena DeBeer
Keyword(s):  
Greenhouse Gas ◽  
Spectroscopic Investigation ◽  
Liquid Fuel ◽  
Methane Monooxygenase ◽  
Enzymatic Conversion ◽  
Particulate Methane Monooxygenase ◽  
X Ray ◽  
Mild Conditions ◽  
Copper Sites ◽  
X Ray Absorption

The enzymatic conversion of the greenhouse gas, methane, to a liquid fuel, methanol, is performed by methane monooxygenases (MMOs) under mild conditions. The copper stoichiometry of particulate MMO (pMMO) has...

scholarly journals Born out of Fire and Ice: Polymorph Studies of the Antiviral Famciclovir

Crystals ◽  
2021 ◽  
Vol 11 (2) ◽  
pp. 129
Author(s):  
Liana Vella-Zarb ◽  
Ulrich Baisch
Keyword(s):  
Variable Temperature ◽  
Chemical Properties ◽  
Crystal Form ◽  
X Ray Diffraction ◽  
Crystal Forms ◽  
X Ray ◽  
Physical Chemical ◽  
Diffraction Patterns ◽  
Crystalline Forms

There is much interest and focus on solid forms of famciclovir. However, in spite of the abundance of reported differences in oral bioavailability, compressibility, and other physical–chemical properties of the various crystal forms of this drug, very little precise structural analysis is available in the literature to date. The form used in the commercial formulation is the anhydrous form I. Patents and patent applications report three different anhydrous crystalline forms on the basis of unindexed powder diffraction patterns. Single-crystal and variable-temperature X-ray diffraction experiments using the commercially available anhydrous form of famciclovir were carried out and led not only to the crystal structure determination of the anhydrous form I, but also to discovery of a new crystal form of anhydrous famciclovir from powder data.

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