Molecular basis for the increased activity of ZMS-2 serine protease in the presence of metal ions and hydrogen peroxide
J Inorg Biochem. 2024 Apr 21;256:112566. doi: 10.1016/j.jinorgbio.2024.112566. Online ahead of print.ABSTRACTSerine proteases are important enzymes widely used in commercial products and industry. Recently, we identified a new serine protease from the desert bacterium Bacillus subtilis ZMS-2 that showed enhanced activity in the presence of Zn2+, Ag+, or H2O2. However, the molecular basis underlying this interesting property is unknown. Here, we report comparative studies between the ZMS-2 protease and its homolog, subtilisin E (SubE), from B. subtilis ATCC 6051. In the absence of Zn2+, Ag+, or H2O2, both enzymes showed the...
Source: Journal of Inorganic Biochemistry - April 24, 2024 Category: Biochemistry Authors: Zahoor Khan Samuel Tanoeyadi Nusrat Jabeen Maryam Shafique Sehar Afshan Naz Taifo Mahmud Source Type: research
Recent mechanistic developments for cytochrome c nitrite reductase, the key enzyme in the dissimilatory nitrate reduction to ammonium pathway
J Inorg Biochem. 2024 Mar 24;256:112542. doi: 10.1016/j.jinorgbio.2024.112542. Online ahead of print.ABSTRACTCytochrome c nitrite reductase, NrfA, is a soluble, periplasmic pentaheme cytochrome responsible for the reduction of nitrite to ammonium in the Dissimilatory Nitrate Reduction to Ammonium (DNRA) pathway, a vital reaction in the global nitrogen cycle. NrfA catalyzes this six-electron and eight-proton reduction of nitrite at a single active site with the help of its quinol oxidase partners. In this review, we summarize the latest progress in elucidating the reaction mechanism of ammonia production, including new find...
Source: Journal of Inorganic Biochemistry - April 17, 2024 Category: Biochemistry Authors: Krystina Hird Julius O Campeci ño Nicolai Lehnert Eric L Hegg Source Type: research
Recent mechanistic developments for cytochrome c nitrite reductase, the key enzyme in the dissimilatory nitrate reduction to ammonium pathway
J Inorg Biochem. 2024 Mar 24;256:112542. doi: 10.1016/j.jinorgbio.2024.112542. Online ahead of print.ABSTRACTCytochrome c nitrite reductase, NrfA, is a soluble, periplasmic pentaheme cytochrome responsible for the reduction of nitrite to ammonium in the Dissimilatory Nitrate Reduction to Ammonium (DNRA) pathway, a vital reaction in the global nitrogen cycle. NrfA catalyzes this six-electron and eight-proton reduction of nitrite at a single active site with the help of its quinol oxidase partners. In this review, we summarize the latest progress in elucidating the reaction mechanism of ammonia production, including new find...
Source: Journal of Inorganic Biochemistry - April 17, 2024 Category: Biochemistry Authors: Krystina Hird Julius O Campeci ño Nicolai Lehnert Eric L Hegg Source Type: research
Recent mechanistic developments for cytochrome c nitrite reductase, the key enzyme in the dissimilatory nitrate reduction to ammonium pathway
J Inorg Biochem. 2024 Mar 24;256:112542. doi: 10.1016/j.jinorgbio.2024.112542. Online ahead of print.ABSTRACTCytochrome c nitrite reductase, NrfA, is a soluble, periplasmic pentaheme cytochrome responsible for the reduction of nitrite to ammonium in the Dissimilatory Nitrate Reduction to Ammonium (DNRA) pathway, a vital reaction in the global nitrogen cycle. NrfA catalyzes this six-electron and eight-proton reduction of nitrite at a single active site with the help of its quinol oxidase partners. In this review, we summarize the latest progress in elucidating the reaction mechanism of ammonia production, including new find...
Source: Journal of Inorganic Biochemistry - April 17, 2024 Category: Biochemistry Authors: Krystina Hird Julius O Campeci ño Nicolai Lehnert Eric L Hegg Source Type: research
Synthesis of substituted terpyridine nickel nitrate complexes and their inhibitory selectivity against cancer cell lines
J Inorg Biochem. 2024 Apr 9;256:112554. doi: 10.1016/j.jinorgbio.2024.112554. Online ahead of print.ABSTRACTSix terpyridine‑nickel complexes 1-6 were formed by the coordination of 4'-(4-R-phenyl)-2,2':6',2″-terpyridine (R = hydroxyl (L1), methoxyl (L2), methylsulfonyl (L3), fluoro (L4), bromo (L5), iodo (L6)) derivatives to nickel nitrate. The compositions and structures of these complexes were analyzed by Fourier Transform infrared spectroscopy (FT-IR), elemental analyses, electrospray ionization mass spectra (ESI-MS), solid-state ultraviolet-visible (UV-Vis) spectroscopy, and single crystal X-ray diffraction (1, 2 an...
Source: Journal of Inorganic Biochemistry - April 13, 2024 Category: Biochemistry Authors: Xin Huang Benwei Wang Dameng Sun Min Chen Xingyong Xue Hongming Liu Yanling Zhou Zhen Ma Source Type: research
Synthesis of substituted terpyridine nickel nitrate complexes and their inhibitory selectivity against cancer cell lines
J Inorg Biochem. 2024 Apr 9;256:112554. doi: 10.1016/j.jinorgbio.2024.112554. Online ahead of print.ABSTRACTSix terpyridine‑nickel complexes 1-6 were formed by the coordination of 4'-(4-R-phenyl)-2,2':6',2″-terpyridine (R = hydroxyl (L1), methoxyl (L2), methylsulfonyl (L3), fluoro (L4), bromo (L5), iodo (L6)) derivatives to nickel nitrate. The compositions and structures of these complexes were analyzed by Fourier Transform infrared spectroscopy (FT-IR), elemental analyses, electrospray ionization mass spectra (ESI-MS), solid-state ultraviolet-visible (UV-Vis) spectroscopy, and single crystal X-ray diffraction (1, 2 an...
Source: Journal of Inorganic Biochemistry - April 13, 2024 Category: Biochemistry Authors: Xin Huang Benwei Wang Dameng Sun Min Chen Xingyong Xue Hongming Liu Yanling Zhou Zhen Ma Source Type: research
Synthesis of substituted terpyridine nickel nitrate complexes and their inhibitory selectivity against cancer cell lines
J Inorg Biochem. 2024 Apr 9;256:112554. doi: 10.1016/j.jinorgbio.2024.112554. Online ahead of print.ABSTRACTSix terpyridine‑nickel complexes 1-6 were formed by the coordination of 4'-(4-R-phenyl)-2,2':6',2″-terpyridine (R = hydroxyl (L1), methoxyl (L2), methylsulfonyl (L3), fluoro (L4), bromo (L5), iodo (L6)) derivatives to nickel nitrate. The compositions and structures of these complexes were analyzed by Fourier Transform infrared spectroscopy (FT-IR), elemental analyses, electrospray ionization mass spectra (ESI-MS), solid-state ultraviolet-visible (UV-Vis) spectroscopy, and single crystal X-ray diffraction (1, 2 an...
Source: Journal of Inorganic Biochemistry - April 13, 2024 Category: Biochemistry Authors: Xin Huang Benwei Wang Dameng Sun Min Chen Xingyong Xue Hongming Liu Yanling Zhou Zhen Ma Source Type: research
A Co(III)-peroxo-arylboronate complex formed by nucleophilic reaction of a Co(III)-peroxo species
J Inorg Biochem. 2024 Apr 9;256:112552. doi: 10.1016/j.jinorgbio.2024.112552. Online ahead of print.ABSTRACTIn this work, we report the generation and characterization of two new Co(III)-peroxo complexes 2 and 3. 2 is best described as a mononuclear CoIII-(O2) complex that exhibits an 18O-isotope sensitive OO bond stretching vibration at 845(-49) cm-1, indicating a relatively weak peroxo moiety compared to those of other CoIII-(O2) complexes reported previously. Complex 3 is a CoIII-peroxo-arylboronate species having a rare {CoIIIOOBO} five-membered metallocycle, which is structurally characterized using X-ray crystallogra...
Source: Journal of Inorganic Biochemistry - April 12, 2024 Category: Biochemistry Authors: Yan Li Suhashini Handunneththige Wenting He Marat R Talipov Dong Wang Source Type: research
Development of Cu(II) 4-hydroxybenzoylhydrazone complexes that induce mitochondrial DNA damage and mitochondria-mediated apoptosis in liver cancer
In this study, two novel Cu(II) complexes (Cu1 and Cu2) were designed and synthesized. Notably, these Cu(II) complexes showed higher cytotoxicity against HL-7402 cells than cisplatin. Moreover, Cu(II) complexes significantly inhibited liver cancer growth in a xenograft model. A mechanism study revealed that the Cu(II) complexes reduced the mitochondrial membrane potential of cancer cells, produced excessive reactive oxygen species (ROS), induced mitochondrial DNA (mtDNA) damage, and ultimately facilitated cancer cell apoptosis.PMID:38599004 | DOI:10.1016/j.jinorgbio.2024.112550 (Source: Journal of Inorganic Biochemistry)
Source: Journal of Inorganic Biochemistry - April 10, 2024 Category: Biochemistry Authors: Ming Jiang Qiwei Yan Yuanping Fu Lili Meng Shuangshuang Gai Xiaohui Pan Yiming Qin Caiyun Jiang Source Type: research
Development of Cu(II) 4-hydroxybenzoylhydrazone complexes that induce mitochondrial DNA damage and mitochondria-mediated apoptosis in liver cancer
In this study, two novel Cu(II) complexes (Cu1 and Cu2) were designed and synthesized. Notably, these Cu(II) complexes showed higher cytotoxicity against HL-7402 cells than cisplatin. Moreover, Cu(II) complexes significantly inhibited liver cancer growth in a xenograft model. A mechanism study revealed that the Cu(II) complexes reduced the mitochondrial membrane potential of cancer cells, produced excessive reactive oxygen species (ROS), induced mitochondrial DNA (mtDNA) damage, and ultimately facilitated cancer cell apoptosis.PMID:38599004 | DOI:10.1016/j.jinorgbio.2024.112550 (Source: Journal of Inorganic Biochemistry)
Source: Journal of Inorganic Biochemistry - April 10, 2024 Category: Biochemistry Authors: Ming Jiang Qiwei Yan Yuanping Fu Lili Meng Shuangshuang Gai Xiaohui Pan Yiming Qin Caiyun Jiang Source Type: research
Development of Cu(II) 4-hydroxybenzoylhydrazone complexes that induce mitochondrial DNA damage and mitochondria-mediated apoptosis in liver cancer
In this study, two novel Cu(II) complexes (Cu1 and Cu2) were designed and synthesized. Notably, these Cu(II) complexes showed higher cytotoxicity against HL-7402 cells than cisplatin. Moreover, Cu(II) complexes significantly inhibited liver cancer growth in a xenograft model. A mechanism study revealed that the Cu(II) complexes reduced the mitochondrial membrane potential of cancer cells, produced excessive reactive oxygen species (ROS), induced mitochondrial DNA (mtDNA) damage, and ultimately facilitated cancer cell apoptosis.PMID:38599004 | DOI:10.1016/j.jinorgbio.2024.112550 (Source: Journal of Inorganic Biochemistry)
Source: Journal of Inorganic Biochemistry - April 10, 2024 Category: Biochemistry Authors: Ming Jiang Qiwei Yan Yuanping Fu Lili Meng Shuangshuang Gai Xiaohui Pan Yiming Qin Caiyun Jiang Source Type: research
Kinetic, electrochemical and spectral characterization of bacterial and archaeal rusticyanins; unexpected stability issues and consequences for applications in biotechnology
J Inorg Biochem. 2024 Mar 25;256:112539. doi: 10.1016/j.jinorgbio.2024.112539. Online ahead of print.ABSTRACTMotivated by the ambition to establish an enzyme-driven bioleaching pathway for copper extraction, properties of the Type-1 copper protein rusticyanin from Acidithiobacillus ferrooxidans (AfR) were compared with those from an ancestral form of this enzyme (N0) and an archaeal enzyme identified in Ferroplasma acidiphilum (FaR). While both N0 and FaR show redox potentials similar to that of AfR their electron transport rates were significantly slower. The lack of a correlation between the redox potentials and electron...
Source: Journal of Inorganic Biochemistry - April 9, 2024 Category: Biochemistry Authors: Liam A Wilson Jamie N Melville Marcelo M Pedroso Stefan Krco Robert Hoelzle Julian Zaugg Gordon Southam Bernardino Virdis Paul Evans Jenna Supper Jeffrey R Harmer Gene Tyson Alice Clark Gerhard Schenk Paul V Bernhardt Source Type: research
Exploiting Principal Component Analysis (PCA) to reveal temperature, buffer and metal ions' role in neuromelanin (NM) synthesis by dopamine (DA) oxidative polymerization
J Inorg Biochem. 2024 Apr 6;256:112548. doi: 10.1016/j.jinorgbio.2024.112548. Online ahead of print.ABSTRACTNeuromelanin (NM) plays a well-established role in neurological disorders pathogenesis; the mechanism of action is still discussed and the investigations in this field are limited by NM's complex and heterogeneous composition, insolubility, and low availability from human brains. An alternative can be offered by synthetic NM obtained from dopamine (DA) oxidative polymerization; however, a deep knowledge of the influence of both physicochemical parameters (T, pH, ionic strength) and other compounds in the reaction med...
Source: Journal of Inorganic Biochemistry - April 9, 2024 Category: Biochemistry Authors: Fabio Schifano Lisa Rita Magnaghi Enrico Monzani Luigi Casella Raffaela Biesuz Source Type: research
Interaction with CT-DNA and in vitro cytotoxicity of two new copper(II)-based potential drugs derived from octanoic hydrazide ligands
J Inorg Biochem. 2024 Mar 28;256:112546. doi: 10.1016/j.jinorgbio.2024.112546. Online ahead of print.ABSTRACTTwo copper(II) complexes [Cu(Hpmoh)(NO3)(NCS)] (1) and [Cu(peoh)(N3)]2 (2) were designed and synthesized by reaction of Cu(NO3)2·3H2O with hydrazone Schiff base ligands,abbreviated with Hpmoh and Hpeoh. Hpmoh and Hpeoh were prepared by condensation reaction of octanoic hydrazide with pyridine-2-carboxyaldehyde and 2-acetylpyridine, respectively. Complexes 1 and 2 were characterized using different analytical techniques such as FT-IR, UV-Vis, IR, EPR and single X-ray diffraction (XRD) analyses as well as computation...
Source: Journal of Inorganic Biochemistry - April 9, 2024 Category: Biochemistry Authors: Manas Chowdhury Niladri Biswas Sandeepta Saha Ashikur Rahaman Poulami Sen Gupta Ankur Banerjee Deba Prasad Mandal Shamee Bhattacharjee Ennio Zangrando Giuseppe Sciortino Federico Pisanu Eugenio Garribba Ruma Roy Choudhury Chirantan Roy Choudhury Source Type: research
Kinetic, electrochemical and spectral characterization of bacterial and archaeal rusticyanins; unexpected stability issues and consequences for applications in biotechnology
J Inorg Biochem. 2024 Mar 25;256:112539. doi: 10.1016/j.jinorgbio.2024.112539. Online ahead of print.ABSTRACTMotivated by the ambition to establish an enzyme-driven bioleaching pathway for copper extraction, properties of the Type-1 copper protein rusticyanin from Acidithiobacillus ferrooxidans (AfR) were compared with those from an ancestral form of this enzyme (N0) and an archaeal enzyme identified in Ferroplasma acidiphilum (FaR). While both N0 and FaR show redox potentials similar to that of AfR their electron transport rates were significantly slower. The lack of a correlation between the redox potentials and electron...
Source: Journal of Inorganic Biochemistry - April 9, 2024 Category: Biochemistry Authors: Liam A Wilson Jamie N Melville Marcelo M Pedroso Stefan Krco Robert Hoelzle Julian Zaugg Gordon Southam Bernardino Virdis Paul Evans Jenna Supper Jeffrey R Harmer Gene Tyson Alice Clark Gerhard Schenk Paul V Bernhardt Source Type: research
