Journal of the American Chemical Society.

Periodical
Chemistry
Publisher:
American Chemical Society. Washington, DC : American Chemical Society
Frequency: Fifty one no. a year, 1993-
Country: United States
Language: English
Author(s):
American Chemical Society., American Chemical Society.
Start Year:1879 -
ISSN:
0002-7863 (Print)
1520-5126 (Electronic)
0002-7863 (Linking)
Impact Factor
15
2022
NLM ID:7503056
(DNLM):J11460000(s)
(OCoLC):01226990
Coden:JACSAT
LCCN:16003159
Classification:W1 JO908G
Fast Fluoroalkylation of Proteins Uncovers the Structure and Dynamics of Biological Macromolecules.
Journal of the American Chemical Society    November 30, 2021   Volume 143, Issue 49 20670-20679 doi: 10.1021/jacs.1c07771
Fojtu00edk L, Fiala J, Pompach P, Chmelu00edk J, Matouu0161ek V, Beier P, Kukau010dka Z, Novu00e1k P.Covalent labeling of proteins in combination with mass spectrometry has been established as a complementary technique to classical structural methods, such as X-ray, NMR, or cryogenic electron microscopy (Cryo-EM), used for protein structure determination. Although the current covalent labeling techniques enable the protein solvent accessible areas with sufficient spatial resolution to be monitored, there is still high demand for alternative, less complicated, and inexpensive approaches. Here, we introduce a new covalent labeling method based on fast fluoroalkylation of proteins (FFAP). FFAP u...
The distal pocket histidine residue in horse heart myoglobin directs the O-binding mode of nitrite to the heme iron.
Journal of the American Chemical Society    November 21, 2009   Volume 131, Issue 50 18119-18128 doi: 10.1021/ja904726q
Yi J, Heinecke J, Tan H, Ford PC, Richter-Addo GB.It is now well-established that mammalian heme proteins are reactive with various nitrogen oxide species and that these reactions may play significant roles in mammalian physiology. For example, the ferrous heme protein myoglobin (Mb) has been shown to reduce nitrite (NO(2)(-)) to nitric oxide (NO) under hypoxic conditions. We demonstrate here that the distal pocket histidine residue (His64) of horse heart metMb(III) (i.e., ferric Mb(III)) has marked effects on the mode of nitrite ion coordination to the iron center. X-ray crystal structures were determined for the mutant proteins metMb(III) H...
Comparative structural and chemical studies of ferritin cores with gradual removal of their iron contents.
Journal of the American Chemical Society    May 29, 2008   Volume 130, Issue 25 8062-8068 doi: 10.1021/ja800492z
Gu00e1lvez N, Fernu00e1ndez B, Su00e1nchez P, Cuesta R, Ceolu00edn M, Clemente-Leu00f3n M, Trasobares S, Lu00f3pez-Haro M, Calvino JJ, Stu00e9phan O....Transmission Electron Microscopy (TEM), X-ray Absorption Near Edge Spectroscopy (XANES), Electron Energy-Loss Spectroscopy (EELS), Small-Angle X-ray Scattering (SAXS), and SQUID magnetic studies were performed in a batch of horse spleen ferritins from which iron had been gradually removed, yielding samples containing 2200, 1200, 500, and 200 iron atoms. Taken together, findings obtained demonstrate that the ferritin iron core consists of a polyphasic structure (ferrihydrite, magnetite, hematite) and that the proportion of phases is modified by iron removal. Thus, the relative amount of magneti...
Solution NMR determination of the seating(s) of meso-nitro-etioheme-1 in myoglobin: implications for steric constraints to meso position access in heme degradation by coupled oxidation.
Journal of the American Chemical Society    August 17, 2001   Volume 123, Issue 33 8080-8088 doi: 10.1021/ja010651a
Wang J, Li Y, Ma D, Kalish H, Balch AL, La Mar GN.The highly stereoselective cleavage of hemin in myoglobin by coupled oxidation has been attributed to steric barriers that leave more space near the alpha- than the other meso-positions. The steric barriers near meso positions in myoglobin have been investigated by establishing the thermodynamics and dynamics of possible seatings in the pocket of horse myoglobin of a four-fold symmetric etioheme I modified with a bulky nitro group at a single meso position. The cyanomet complex of this reconstituted myoglobin exhibits three sets of (1)H NMR resonances that are linked dynamically and occur in a...
Dynamics of structure and energy of horse carboxymyoglobin after photodissociation of carbon monoxide.
Journal of the American Chemical Society    July 18, 2001   Volume 123, Issue 18 4286-4294 doi: 10.1021/ja9944655
Sakakura M, Yamaguchi S, Hirota N, Terazima M.The energetics and structural volume changes after photodissociation of carboxymyoglobin are quantitatively investigated by laser-induced transient grating (TG) and photoacoustic calorimetric techniques. Various origins of the TG signal are distinguished: the phase grating signals due to temperature change, due to absorption spectrum change, and due to volume change. We found a new kinetics of approximately 700 ns (at room temperature), which was not observed by the flash photolysis technique. This kinetics should be attributed to the intermediate between the geminate pair and the fully dissoc...
Electron-transfer protein reactivities. Kinetic studies of the oxidation of horse heart cytochrome c, Chromatium vinosum high potential iron-sulfur protein, Pseudomonas aeruginosa azurin, bean plastocyanin, and Rhus vernicifera stellacyanin by pentaamminepyridineruthenium(III).
Journal of the American Chemical Society    July 20, 1977   Volume 99, Issue 15 5158-5167 doi: 10.1021/ja00457a042
Cummins D, Gray HB.No abstract available
Letter: Kinetics of reduction of horse-heart ferricytochrome c by catechol.
Journal of the American Chemical Society    June 23, 1976   Volume 98, Issue 13 4023-4024 doi: 10.1021/ja00429a061
Toppen DL.No abstract available
Kinetic studies of the oxidation and reduction of Chromatium high potential iron-sulfur protein (HiPIP) by inorganic complexes. Comparison of the electron transfer reactivities of HiPIP and horse heart cytochrome c.
Journal of the American Chemical Society    April 14, 1976   Volume 98, Issue 8 2177-2180 doi: 10.1021/ja00424a028
Rawlings J, Wherland S, Gray HB.No abstract available
Synthetic peptides related to horse heart cytochrome c. VII. Synthesis and inhibitory properties of the 70-80 undecapeptide.
Journal of the American Chemical Society    March 8, 1972   Volume 94, Issue 5 1720-1723 doi: 10.1021/ja00760a050
Wolman Y, Schejter A, Sokolovsky M.No abstract available
Physical, chemical and immunological properties of phosphorylated crystalline horse serum albumin.
Journal of the American Chemical Society    January 1, 1946   Volume 68 18-25 doi: 10.1021/ja01205a007
MAYER M, HEIDELBERGER M.No abstract available