[NMR paper] Ferrous Iron Binding Key to Mms6 Magnetite Biomineralisation: A Mechanistic Study to Understand Magnetite Formation Using pH Titration and NMR Spectroscopy.
Ferrous Iron Binding Key to Mms6 Magnetite Biomineralisation: A Mechanistic Study to Understand Magnetite Formation Using pH Titration and NMR Spectroscopy.
Related ArticlesFerrous Iron Binding Key to Mms6 Magnetite Biomineralisation: A Mechanistic Study to Understand Magnetite Formation Using pH Titration and NMR Spectroscopy.
Abstract
Formation of magnetite nanocrystals by magnetotactic bacteria is controlled by specific proteins which regulate the particles' nucleation and growth. One such protein is Mms6. This small, amphiphilic protein can self-assemble and bind ferric ions to aid in magnetite formation. To understand the role of Mms6 during in vitro iron oxide precipitation we have performed in situ pH titrations. We find Mms6 has little effect during ferric salt precipitation, but exerts greatest influence during the incorporation of ferrous ions and conversion of this salt to mixed-valence iron minerals, suggesting Mms6 has a hitherto unrecorded ferrous iron interacting property which promotes the formation of magnetite in ferrous-rich solutions. We show ferrous binding to the DEEVE motif within the C-terminal region of Mms6 by NMR spectroscopy, and model these binding events using molecular simulations. We conclude that Mms6 functions as a magnetite nucleating protein under conditions where ferrous ions predominate.
PMID: 27112228 [PubMed - as supplied by publisher]
[NMR paper] The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
http://www.bionmr.com//www.ncbi.nlm.nih.gov/corehtml/query/egifs/http:--highwire.stanford.edu-icons-externalservices-pubmed-highwire.gif Related Articles The N-terminal ubiquitin-binding region of ubiquitin-specific protease 28 modulates its deubiquitination function: NMR structural and mechanistic insights.
Biochem J. 2015 Oct 15;471(2):155-65
Authors: Wen Y, Shi L, Ding Y, Cui R, He WT, Hu HY,...
[NMR paper] Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
Related Articles Electrostatic interactions in the binding pathway of a transient protein complex studied by NMR and isothermal titration calorimetry.
J Biol Chem. 2014 Aug 13;
Authors: Meneses E, Mittermaier A
Abstract
Much of our knowledge of protein binding pathways is derived from extremely stable complexes that interact very tightly, with lifetimes of hours to days. Much less is known about...
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[NMR paper] Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
Mechanistic Insight into the Relationship between N-Terminal Acetylation of ?-Synuclein and Fibril Formation Rates by NMR and Fluorescence.
PLoS One. 2013;8(9):e75018
Authors: Kang L, Janowska MK, Moriarty GM, Baum J
Abstract
Aggregation of ?-synuclein (?Syn), the primary protein component in Lewy body inclusions of patients with Parkinson's disease, arises when the normally soluble intrinsically...
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NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
NMR structure note: the ferrous iron transport protein C (FeoC) from Klebsiella pneumoniae
Content Type Journal Article
Category NMR structure note
Pages 1-5
DOI 10.1007/s10858-012-9633-6
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NMR Study on the B–ZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
NMR Study on the B–ZJunction Formation ofDNA Duplexes Induced by Z-DNA Binding Domain of Human ADAR1
Yeon-Mi Lee, Hee-Eun Kim, Chin-Ju Park, Ae-Ree Lee, Hee-Chul Ahn, Sung Jae Cho, Kwang-Ho Choi, Byong-Seok Choi and Joon-Hwa Lee
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja211581b/aop/images/medium/ja-2011-11581b_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja211581b
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http://feeds.feedburner.com/~r/acs/jacsat/~4/9iGipRMHcHU
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Mechanistic Studies of the Lithium Enolate of 4-Fluoroacetophenone: Rapid-Injection NMR Study of Enolate Formation, Dynamics, and Aldol Reactivity
Mechanistic Studies of the Lithium Enolate of 4-Fluoroacetophenone: Rapid-Injection NMR Study of Enolate Formation, Dynamics, and Aldol Reactivity
Kristopher J. Kolonko, Daniel J. Wherritt and Hans J. Reich
http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jacsat/0/jacsat.ahead-of-print/ja207218f/aop/images/medium/ja-2011-07218f_0005.gif
Journal of the American Chemical Society
DOI: 10.1021/ja207218f
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[NMR paper] Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
Related Articles Iron uptake by ferritin: NMR relaxometry studies at low iron loads.
J Inorg Biochem. 1998 Sep;71(3-4):153-7
Authors: Vymazal J, Brooks RA, Bulte JW, Gordon D, Aisen P
Twenty ferritin samples were prepared at pH 6.5 with average loadings of 0-89 Fe atoms per molecule. Nuclear magnetic relaxation times T1 and T2 were measured at 3 degrees C, 23 degrees C, and at 37 degrees C and at field strength from 0.025 to 1.5 T. The field dependence, temperature dependence,...