Results 101 to 110 of about 339,218 (339)

Heme and immunity: The heme oxygenase dichotomy

Journal of Inorganic Biochemistry
Heme, an iron containing organic ring, is required for a diverse range of biological processes across all forms of life. Although this nutrient is essential, its pro-inflammatory and cytotoxic properties can lead to cellular damage. Heme oxygenase 1 (HO-1) is an endoplasmic reticulum (ER)-anchored enzyme that degrades heme, releasing equimolar amounts ...
Melissa, Perry, Iqbal, Hamza
openaire   +2 more sources

Breaking the Selectivity Barrier of Single‐Atom Nanozymes Through Out‐of‐Plane Ligand Coordination

Advanced Materials, EarlyView.
Here, Ru SAzyme with out‐of‐plane chlorine ligands is reported as a monofunctional, high‐performance peroxidase‐like nanozyme. Incorporating out‐of‐plane ligand coordination emulates enzyme selectivity and regulates reaction pathways for an identical substrate.
Seonhye Park, Kyu In Shim, Phuong Thy Nguyen, Daeeun Choi, Seongbeen Kim, Seung Yeop Yi, Moon Il Kim, Jeong Woo Han, Jinwoo Lee   +8 more
wiley   +1 more source

Import of apocytochrome c into the mitochondrial intermembrane space along a cytochrome c1 sorting pathway [PDF]

, 1990
The question of whether cytochrome c could be functionally sorted to the mitochondrial intermembrane space along a "conservative sorting" pathway was investigated using a fusion protein termed pLc1-c. pLc1-c contains 3-fold targeting information, namely,
Neupert, Walter, Nicholson, Donald W., Stuart, Rosemary A., Wienhues, Ulla   +3 more
core  

Resonance Raman Spectroscopy Reveals pH-Dependent Active Site Structural Changes of Lactoperoxidase Compound 0 and Its Ferryl Heme O–O Bond Cleavage Products [PDF]

, 2014
The first step in the enzymatic cycle of mammalian peroxidases, including lactoperoxidase (LPO), is binding of hydrogen peroxide to the ferric resting state to form a ferric-hydroperoxo intermediate designated as Compound 0, the residual proton ...
Kincaid, James R., Mak, Piotr J., Thammawichai, Warut, Wiedenhoeft, Dennis   +3 more
core   +3 more sources

Spatial Coordination Structure‐Driven Enzyme‐Like Selectivity in Single‐Atom Nanozymes

Advanced Materials, EarlyView.
Sun et al. reviews recent progress in enhancing the enzyme‐like catalytic selectivity of SAzymes through the rational design of their spatial coordination structures. They emphasize the structure‐activity relationships of various attributes of these coordination structures in promoting selective catalytic behavior, the strategic design of coordination ...
Qijun Sun, Si Liu, Ziping Li, Peiji Deng, Na Niu, Ligang Chen, Kang Liang   +6 more
wiley   +1 more source

Heme oxygenase-1 as a modulator of intestinal inflammation development and progression [PDF]

, 2018
Indexación: Scopus.Heme Oxygenase 1 (HMOX1) is an enzyme that catalyzes the reaction that degrades the heme group contained in several important proteins, such as hemoglobin, myoglobin, and cytochrome p450.
Alexis M. Kalergis, Alexis M. Kalergis, Bárbara M. Schultz, Claudia A. Riedel, Geraldyne A. Salazar, Irenice Coronado-Arrázola, Loni Berkowitz, Loni Berkowitz, Manuel M. Álvarez-Lobos, Manuel M. Álvarez-Lobos, Omar P. Vallejos, Susan M. Bueno, Valentina P. Sebastián   +12 more
core   +2 more sources

Integrating Visible‐Light Photocatalysis and Enzymes for the Stereoselective Synthesis of Alcohols and Amines

Advanced Synthesis &Catalysis, EarlyView.
The integration between visible‐light photocatalysis and biocatalysis has the potential to greatly improve modern organic synthesis by combining the production of valuable synthetic intermediates under mild photochemical conditions with the high degree of stereoselectivity reached by enzymes. The review collects the recent efforts in the photoenzymatic
Stefano Parisotto, Cristina Prandi
wiley   +1 more source

Role of cytochrome c heme lyase in the import of cytochrome c into mitochondria [PDF]

, 1988
The import of cytochrome c into Neurospora crassa mitochondria was examined at distinct stages in vitro. The precursor protein, apocytochrome c, binds to mitochondria with high affinity and specificity but is not transported completely across the outer ...
Hergersberg, Christoph, Neupert, Walter, Nicholson, Donald W.   +2 more
core  

The effects of nitroxyl (HNO) on soluble guanylate cyclase activity: interactions at ferrous heme and cysteine thiols [PDF]

, 2009
It has been previously proposed that nitric oxide (NO) is the only biologically relevant nitrogen oxide capable of activating the enzyme soluble guanylate cyclase (sGC). However, recent reports implicate HNO as another possible activator of sGC.
Adrian J. Hobbs, Anderegg, Andrea J. Lee, Bari, Bartberger, Bermejo, Bonner, Brandwein, Burstyn, Craven, Craven, De Witt, DeMaster, Denninger, Derbyshire, DeRubertis, Dierks, Doyle, Drago, Dutton, Dutton, Ellis, Ellis, Farmer, Favaloro, Feelisch, Fukuto, Fukuto, Haddox, Halliwell, Hobbs, Hoshino, Ignarro, Ignarro, Ignarro, Ignarro, Immoos, Irvine, Irvine, Jon M. Fukuto, Judith N. Burstyn, Kamisaki, Katrina M. Miranda, Kim, Lin, Lopez, Maragos, Melisa M. Cherney, Miranda, Miranda, Miranda, Nestor E. Francoleon, Niederhoffer, Paolocci, Paolocci, Patrick J. Farmer, Pervitsky, Pino, Poulos, Rusche, S. Bruce King, Sayed, Scheidt, Schmidt, Serfass, Sha, Shafirovich, Shahidullah, Shen, Smith, Stasch, Stone, Stone, Sulc, Sulc, Thadani, Thomas W. Miller, Turk, Väänänen, Väänänen, Wanstall, Wayland, Wayland, Wolin, Wong, Yonetani   +85 more
core   +2 more sources

The Role of Bilirubin and the Other “Yellow Players” in Neurodegenerative Diseases

Antioxidants, 2020
Bilirubin is a yellow endogenous derivate of the heme catabolism. Since the 1980s, it has been recognized as one of the most potent antioxidants in nature, able to counteract 10,000× higher intracellular concentrations of H2O2.
Sri Jayanti, Libor Vítek, Claudio Tiribelli, Silvia Gazzin   +3 more
doaj   +1 more source