Metalloproteins and Heme Structures

Which of the following best describes the role of metal ions in oxidation-reduction reactions within metalloproteins?

How does the binding of oxygen to hemoglobin affect its spectroscopic properties, specifically the Soret band?

In restriction enzymes, what is the primary role of magnesium ions ($Mg^{2+}$) at the active site?

What is the role of metal ions in proteins that act on phosphate-containing substrates?

How does the presence of a metal ion, like zinc, contribute to the function of enzymes such as alcohol dehydrogenase (ADH)?

What is the significance of the iron-containing heme group in catalase?

How do superoxide dismutases (SODs) protect cells from oxidative stress?

What is the role of selenium in glutathione peroxidase?

In the context of cytochrome P-450 monooxygenase systems, what is the role of the heme group?

How does $Mg^{2+}$ function as a cofactor for kinases?

[Blank] are proteins that contain a metal ion cofactor, which is essential for their biological functions.

The primary structure of a protein refers to the sequence of ______ linked together by peptide bonds.

Secondary structure in proteins involves the formation of local structures such as alpha helices and beta sheets, stabilized by ______ bonds between the backbone atoms.

Tertiary structure describes the overall three-dimensional arrangement of all atoms in a single polypeptide chain, stabilized by various interactions including hydrophobic interactions, disulfide bonds, and ______ bonds.

Quaternary structure refers to the arrangement of multiple ______ subunits in a multi-subunit protein complex.

Metals in proteins can ______ ligands and substrates, facilitating their interaction and reaction within the protein's active site.

Many metalloproteins mediate oxidation-______ reactions by changing the oxidation state of the metal ion at their active site.

Metals provide ______ stabilization in proteins by compensating for negative or positive charges, which is crucial for maintaining the proper folding and function of the protein.

Certain metalloproteins promote ______ catalysis by increasing the nucleophilicity of reactants, thereby accelerating chemical reactions.

[Blank]is a porphyrin ring complexed with iron, found in hemoglobin, myoglobin, and cytochromes.

In hemoglobin, the binding of oxygen alters the position of the ______ band, which can be observed using UV-Vis spectrophotometry.

[Blank], which appears purplish/blueish in color, is dominant in venous blood, while oxyhemoglobin, which appears red, is dominant in arterial blood.

[Blank] enzymes are a class of enzymes that cut DNA molecules at specific, short sequences and require Mg2+ ions.

In restriction enzymes, ______ ions help to reduce electrostatic repulsion and facilitate the orientation of the substrate for effective DNA cleavage.

[Blank] is a post-translational modification involving the addition of a carboxyl group to glutamate residues, often dependent on calcium.

[Blank] catalyzes the oxidation of alcohols to aldehydes or ketones, utilizing a zinc ion at the active site for catalysis.

Reactive oxygen species, including ______, are continuously formed as by-products of aerobic metabolism and can cause oxidative stress if not properly managed.

[Blank] is a common enzyme that catalyzes the decomposition of hydrogen peroxide into water and oxygen, containing iron-containing heme groups.

[Blank] dismutase is a metalloenzyme that protects cells from oxidative stress by catalyzing the dismutation of superoxide radicals into oxygen and hydrogen peroxide.

[Blank] peroxidase utilizes glutathione to reduce hydrogen peroxide to water, playing a critical role in cellular antioxidant defense.

Cytochrome P-450 ______ are involved in the metabolism of steroids, bile acids, and xenobiotics, requiring heme and undergoing redox cycling.

In Cytochrome P-450 systems, the microsomal system is located in the endoplasmic ______ and is particularly involved in xenobiotic metabolism.

The intensity of the Soret band found within a heme group is higher in its Ferrous $(Fe^{2+})$ form, which exhibits maximal light absorption at ______ nm.

The active site of carbonic anhydrase contains ______, which is directly involved in the hydration of carbon dioxide.

Many enzymes that interact with substrates that act upon phosphate groups require $Mg^{2+}$ or other ______ cations to function.

In molecular biology, a ______ bond is a covalent chemical bond that can be broken by an enzyme.

Three forms of superoxide dismutase exist within the body, including SOD1 which exists in the ______, SOD2 which exists in the Mitochondria, and SOD3 which exists in the Extracellular

$[Blank]$ can contain a heme cofactor in their active sites, or alternately redox-active cysteine or selenocysteine residues.

The enzyme [Blank] is capable of catalyzing the decomposition of hydrogen peroxide into water and oxygen.

[Blank] is one of a family of reactive oxygen species formed from the partial reduction of molecular oxygen.

Glutathione Peroxidase, Glutathione Reductase couple enzyme reaction reduces $H_2O_2$ into $2H_2O$ with $2 G-[Blank]$

Cytochrome P-450 monooxygenase systems are further divided into types based on locations in the cell, those being Mitochondrial and [Blank].

Kinases require $Mg^{2+}$ in order to reduce the electrostatic ______ between ATP and Glucose within the active site.

In its oxidized state, Glutathione exists as two $G-SH$ interacting with a ______ bond to create a single $G-S-S-G$ molecule.

Alcohol Dehydrogenase requires $NAD^+$ in order to oxidize alcohols, which will ultimately allow to convert them into organic-acid $[Blank]$.

The Bohr effect is used within [Blank] anhydrase ($H_2CO_3$) to manipulate the acidity.

[Blank] are a class of proteins that contain a tightly bound metal ion as part of their structure, which plays a role in their function.

The secondary structure of a protein, composed of alpha helices and beta sheets, is primarily stabilized by ______ bonds between the carbonyl oxygen and amide hydrogen atoms in the polypeptide backbone.

In metalloproteins, the metal ions are often coordinated by amino acid residues such as histidine, cysteine, and ______, which donate electrons to form a stable complex.

The porphyrin ring in heme is a ______ structure composed of four pyrrole rings linked together, with a central iron ion coordinated by the nitrogen atoms of the pyrrole rings.