Jacob H Artz
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Explore the profile of Jacob H Artz including associated specialties, affiliations and a list of published articles.
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14
Citations
199
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Recent Articles
1.
Kisgeropoulos E, Artz J, Blahut M, Peters J, King P, Mulder D
J Biol Chem
. 2024 Apr;
300(6):107292.
PMID: 38636659
[FeFe]-hydrogenases catalyze the reversible oxidation of H from electrons and protons at an organometallic active site cofactor named the H-cluster. In addition to the H-cluster, most [FeFe]-hydrogenases possess accessory FeS...
2.
Smolinski S, Lubner C, Guo Z, Artz J, Brown K, Mulder D, et al.
RSC Adv
. 2023 Jan;
13(1):742.
PMID: 36683772
[This corrects the article DOI: 10.1039/D2RA01295B.].
3.
Smolinski S, Lubner C, Guo Z, Artz J, Brown K, Mulder D, et al.
RSC Adv
. 2022 Jun;
12(23):14655-14664.
PMID: 35702219
The capacity of cyanobacteria to adapt to highly dynamic photon flux and nutrient availability conditions results from controlled management and use of reducing power, and is a major contributing factor...
4.
A site-differentiated [4Fe-4S] cluster controls electron transfer reactivity of [FeFe]-hydrogenase I
Lubner C, Artz J, Mulder D, Oza A, Ward R, Williams S, et al.
Chem Sci
. 2022 Jun;
13(16):4581-4588.
PMID: 35656134
One of the many functions of reduction-oxidation (redox) cofactors is to mediate electron transfer in biological enzymes catalyzing redox-based chemical transformation reactions. There are numerous examples of enzymes that utilize...
5.
Wise C, Ledinina A, Yuly J, Artz J, Lubner C
Biochim Biophys Acta Bioenerg
. 2021 Jan;
1862(4):148377.
PMID: 33453185
Electron bifurcation is a biological mechanism to drive a thermodynamically unfavorable redox reaction through direct coupling with an exergonic reaction. This process allows microorganisms to generate high energy reducing equivalents...
6.
Artz J, Tokmina-Lukaszewska M, Mulder D, Lubner C, Gutekunst K, Appel J, et al.
J Biol Chem
. 2020 May;
295(28):9445-9454.
PMID: 32409585
Cyanobacterial Hox is a [NiFe] hydrogenase that consists of the hydrogen (H)-activating subunits HoxYH, which form a complex with the HoxEFU assembly to mediate reactions with soluble electron carriers like...
7.
Artz J, Zadvornyy O, Mulder D, Keable S, Cohen A, Ratzloff M, et al.
J Am Chem Soc
. 2019 Dec;
142(3):1227-1235.
PMID: 31816235
Hydrogenases display a wide range of catalytic rates and biases in reversible hydrogen gas oxidation catalysis. The interactions of the iron-sulfur-containing catalytic site with the local protein environment are thought...
8.
Ratzloff M, Artz J, Mulder D, Collins R, Furtak T, King P
J Am Chem Soc
. 2018 May;
140(24):7623-7628.
PMID: 29792026
The [FeFe]-hydrogenases ([FeFe] Hases) catalyze reversible H activation at the H-cluster, which is composed of a [4Fe-4S] subsite linked by a cysteine thiolate to a bridged, organometallic [2Fe-2S] ([2Fe]) subsite....
9.
Artz J, Zadvornyy O, Mulder D, King P, Peters J
Methods Enzymol
. 2017 Sep;
595:213-259.
PMID: 28882202
The crystallization of FeS cluster-containing proteins has been challenging due to their oxygen sensitivity, and yet these enzymes are involved in many critical catalytic reactions. The last few years have...
10.
Therien J, Artz J, Poudel S, Hamilton T, Liu Z, Noone S, et al.
Front Microbiol
. 2017 Jul;
8:1305.
PMID: 28747909
The first generation of biochemical studies of complex, iron-sulfur-cluster-containing [FeFe]-hydrogenases and Mo-nitrogenase were carried out on enzymes purified from (strain W5). Previous studies suggested that two distinct [FeFe]-hydrogenases are expressed...